Next Article in Journal
Molecular Regulation of Carotenoid Accumulation Enhanced by Oxidative Stress in the Food Industrial Strain Blakeslea trispora
Previous Article in Journal
Are Insect-Based Foods Healthy? An Evaluation of the Products Sold in European E-Commerce
 
 
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
Review

β-Glucosidase Activity of Lactiplantibacillus plantarum: A Key Player in Food Fermentation and Human Health

by
Gianluca Paventi
1,*,
Catello Di Martino
1,
Francesca Coppola
2 and
Massimo Iorizzo
1,*
1
Department of Agricultural, Environmental and Food Sciences, University of Molise, Via De Sanctis, 86100 Campobasso, Italy
2
Department of Agricultural Sciences, University of Naples “Federico II”, Portici, 80055 Naples, Italy
*
Authors to whom correspondence should be addressed.
Foods 2025, 14(9), 1451; https://doi.org/10.3390/foods14091451
Submission received: 21 March 2025 / Revised: 18 April 2025 / Accepted: 20 April 2025 / Published: 22 April 2025

Abstract

:
β-glucosidases are a relevant class of enzymes in the food industry due to their role in hydrolyzing different types of glycosidic bonds. This activity allows for formation of volatile compounds and release of bioactive aglycone compounds. In addition to endogenous β-glucosidase activity present in raw material, the function of β-glucosidases in fermenting microorganisms has been progressively clarified and increasingly appreciated. In this regard, several lactic acid bacteria, including Lactiplantibacillus plantarum, showed high β-glucosidase activity, which can be considered as a valid biotechnological resource in different food sectors. Here, we reviewed the huge literature in which the β-glucosidases of L. plantarum were shown to play a role, highlighting how their action results in enhancing the nutritional, sensory, and functional properties of fermented foods. To this aim, after a brief introduction of the main functions of these enzymes in several kingdoms, we critically analyzed the involvement of L. plantarum β-glucosidases in plant-based food production, with a particular insight for soy, cassava, and olive-fermented products, as well as in the production of both alcoholic and non-alcoholic beverages. We trust that the reports summarized here can be helpful in planning future research and innovative strategies to obtain pleasing, functional, and healthy foods.

1. Introduction

β-glucosidases are a class of exoglucosidase enzymes capable of acting on terminal non-reducing β-D-glucosyl residues by hydrolyzing the β-1,4 glycosidic bond of different glycoconjugates including glucosides, oligosaccharides, and 1-O-glucosyl esters, with the release of β-D-glucose [1]. Although in some limited cases β-S-glucosidase activity was also reported [2], these enzymes act on O-glycosylated substrates, releasing aglycone compounds. On the basis of their amino acid sequences, they are classified in families and clans that share a conserved catalytic mechanism, structure, and active site residues, but may vary in substrate specificity [3,4]. These enzymes are ubiquitous in nature and are found in all domains of living organisms—Archaea, Eubacteria, and Eukaryotes (fungi, plants, and animals, including humans) [5]. In these organisms, β-glucosidases play a significant role in various biological processes and functions including nutritional acquisition and ecological associations. However, most organisms utilize this enzyme for the hydrolysis of oligosaccharides to glucose, the most usable form of carbon. The β-glucosidases fall in the enzyme class EC 3.2.1.21. At present, 133 glycoside hydrolase (GH) families are listed in the frequently updated Carbohydrate Active enZYme (CAZY) database (http://www.cazy.org, accessed on 19 April 2025) [6]. So far, they have been classified into GH1, GH3, GH5, GH9, and GH30. Family GH1 includes β-glucosidases from archaebacteria, plants, and mammals, and family GH3 comprises β-glucosidases of some bacterial, mold, and yeast origin [7,8,9,10]; GH9 β-glucosidases are reported to differ in their mechanism of action with respect to GH1, GH3, and GH30 family members [10]. Structures and sequences for both GH1 and GH3 β-glucosidases were recently reviewed by Ouyang [11].
In plants, β-glucosidases perform a wide range of biological functions such as pathogen and insect resistance, microbial interactions, lignification, phytohormones activation, signaling mechanisms, cleavage of glycosylated flavonoids, fruit ripening, and pigment metabolism [5,12,13,14,15,16].
In humans, three native β-glucosidase enzymes have been identified: glucocerebrosidase, deficiency of which causes Gaucher’s disease; lactase phlorizin hydrolase, deficiency of which causes lactose intolerance; and β-glucosidase, a cytosolic enzyme of broad specificity that is abundant in the kidney, liver, and small intestine of mammals and plays a crucial role in the transport and/or digestion of dietary sugars [17,18,19].
In insects, β-glucosidases are mainly involved in cellobiose digestion, the breakdown of glucosinolates (glucosylated specialized metabolites) sequestered from host plants to form a dual-component defense system, and communication and recognition among sexual or social interactions. These functions have been found in different groups of insects, and they adapt to the system based on the plants they feed on [20,21].
The genetic diversity and expression of β-glucosidase-producing microorganisms were studied in different habitats, including food, soil, cow dung and compost, and marine environments [22,23,24,25,26,27]. In bacteria and fungi, β-glucosidase is a crucial element of the microbial cellulose multienzyme complex since it is responsible for the regulation of the entire cellulose hydrolysis process by easing cellobiose-mediated suppression and producing the final product glucose [22,28]. The fungal species Aspergillus niger is the major source of commercial β-glucosidase; however, this enzyme has been produced, purified, and characterized from other mold genus (e.g., Trichoderma, Aspergillus, Penicillium, Fusarium, etc.), with the majority of which belonging to GH3 as cited in [29].
In addition, the β-glucosidase has been identified, purified, and characterized from many bacteria (e.g., Clostridium, Bacillus, Paenibacillus, Bifidobacterium, etc.) including some Lactic Acid Bacteria (LAB), as reported in previous reviews and research articles [30,31,32,33]. In particular, the β-glucosidase produced by LABs plays an important role in the performance of these microorganisms in food fermentation or during interaction with their hosts in the intestinal environment, as reported by Michlmayr et al. in a previous review [30]. For example, they have the potential to improve the flavor and aroma of alcoholic (e.g., wine and beer) and non-alcoholic beverages (e.g., teas and juices) by releasing aromatic compounds from flavorless glycosides. Microbial β-glucosidase is also used to hydrolyze isoflavonic glycosides (e.g., soybean products), as well as oleuropein, thus reducing the bitterness of table olives [7].
During food fermentation or by interaction with their hosts, several LAB can provide β-glucosidase activities to increase the bioavailability of metabolites that improve the host health, such as plant phenolic compounds, which are usually glycosylated in their dietary format, and therefore are less bioavailable than the aglycone forms [34,35,36]. A known example includes the soy isoflavones, which can be released from their glycosylated precursors by some LAB β-glucosidases during soy fermentation [37]. The β-glucosidase activities from LAB may also have implications for food security. Cassava contains high concentrations of the toxic cyanogenic glucoside linamarin, and LAB contributes to the degradation of linamarin by β-glucosidase activities [7].
On the other hand, it is known that the mycotoxin deoxynivalenol is not toxic in its glycosylated form (deoxynivalenol-3-glucoside), but it can be activated by a LAB β-glucosidase [38].
Given the importance of LAB β-glucosidases, considerable efforts have been focused to increase our knowledge on these enzymes, which usually show a broad specificity [30].
Among the LAB able to produce β-glycosidases, Lactiplantibacillus plantarum (formerly Lactobacillus plantarum) represents an important member. This heterofermentative species is also known for its high adaptability to many different conditions, since it has been isolated from various ecological niches including milk, fruit, cereal crops, vegetables, bee bread, and fresh meat [39,40,41,42,43], as well as fermented foods [44,45]. Moreover, this species is widely diffused into the gastrointestinal tract of animals; several studies, in fact, showed that it colonizes the digestive system of insects [46,47,48], fish [49], and mammals, including humans [50]. The inclusion of L. plantarum in both QPS (Qualified Presumption of Safety) and GRAS (Generally Recognised as Safe) lists [51,52], together with the many intrinsic properties of this species, led to the proposal of numerous L. plantarum strains as animal and human probiotics [53,54].
L. plantarum is widely used as a starter culture in the fermentation of raw materials of plant and animal origin, where it contributes to enhancing the sensorial quality and shelf-life of fermented products. Some L. plantarum strains also increase the functional properties of various fermented foods by producing a variety of bioactive compounds [55,56].
The present review aims to provide an overview of the role of the activity of β-glycosidase produced by L. plantarum as a valid biotechnological resource in different food sectors. In particular, following a general description of the role/s of β-glycosidase in plant fermented foods, we critically analyzed the involvement of L. plantarum β-glucosidases in plant-based food production, with a particular insight for soy-, cassava-, and olive-fermented products, as well as in the production of both alcoholic and non-alcoholic beverages. Despite β-glycosidases reported to be potentially involved also in thioglycohydrolase activity [2], the main function in L. plantarum-fermented foods can be restricted to its action on O-glycosylated compounds as specificized in the subsequent paragraphs.

2. Roles of β-Glucosidases in Fermented Plant-Based Foods

The natural chemicals of fruit include volatile compounds, both in free and bound form, which occur primarily as glycoconjugates of sugar and an aglycone [57,58]. The sugar moiety includes glucose or a disaccharide, while the aglycone part of glycosides is often represented by monoterpenes, C13-norisoprenoids, benzene derivatives, and long-chain aliphatic alcohols [59,60,61,62]. Therefore, the hydrolysis of odorless glycosylated compounds can make an important contribution to improve the flavor of fruit juices and derived beverages [57]. In this regard, β-glucosidases play a major role since they hydrolyze glycosidic bonds occurring in aroma precursors thus promoting the release of free volatile compounds, as reviewed in [58].
Although endogenous β-glucosidases are present in fruits such as grapes, their activity is insufficient due to low stability under juice processing and winemaking conditions. In fact, the optimal pH levels at which plant glucosidases are most active generally range from 4.0 to 6.0; therefore, in the low pH of fruit juices, only limited activity of most glycosidases has been observed [63,64].
Due to this limited action of plant endogenous glycosidases, a large proportion of the aroma compounds in juices remain inactive, in a glycosidically bound form [65]. Research has therefore focused on finding exogenous sources of glucoside hydrolases, which can be used in the production of juices and wines [65,66].
Several procedures can be used to enhance wine aroma by releasing aroma compounds from glycosidic precursors, including acid or enzymatic hydrolysis. Acid hydrolysis causes rearrangements in the aglycone structure with the formation of undesirable flavors, while enzymatic hydrolysis specifically cleaves the glycosidic linkage without altering the aglycone structure [67].
Glycosidic precursors in fruits can be found as D-glucopyranosides in which the volatile aglycone is linked to a single D-glucopyranose by a β-glycoside bond. They can also occur as disaccharides, in which the D-glucopyranose is combined with a second sugar molecule such as α-L-arabinofuranose, α-L-rhamnopyranose, or α-L-apiofuranose (Figure 1).
The enzymatic hydrolysis of glycosidically bound aroma compounds occurs in two steps and involves different exoglycosidases depending on the sugar moieties of the substrates. For example, in the presence of rhamnose or apiose: first, a α-L-rhamnosidase or a β-D-apiofuranosidase cleaves the (1-6)-glycosidic linkage, and then, the flavor compounds are liberated from the monoglucosides by the action of a β-glucosidase. A hydrolysis scheme of glycosidic aroma precursors is shown in Figure 1.
Therefore, much attention has been attracted to the flavor enhancement of juices or wines through the hydrolysis of the glycoside aroma precursors using microbial β-glucosidases from mold, yeast, and LAB [68,69,70,71].
Phenolics, including flavonoids, widely distributed in plants, have received much attention and were recognized as the most abundant antioxidants in the human diet [72]. Increased antioxidative activity in fermented plant-based foods is primarily due to an increase in the amounts of phenolic compounds and flavonoid aglycones during fermentation, which is the result of a microbial hydrolysis activity [73].
Flavonoids are the largest class of polyphenols that can be further categorized into several subgroups including flavonols and anthocyanins, both of which are naturally distributed in plant foods as glycosides containing single or multiple sugar moieties. Flavonoid aglycones are generally more bioavailable than their respective glycosides [74].
Several studies have shown that flavonoid aglycones’ content in plant-based foods can increase after fermentation due to the microbial β-glucosidase. Therefore, fermentation by LAB possessing this specific enzymatic activity is an effective strategy to increase the bioavailability of natural antioxidants present in fermented plant-based products [75]. In this regard, the selection and use of probiotic starters, besides the production of fermented dairy products [76], represents an important biotechnological tool to be applied more widely, especially in the field of plant-derived fermented products [42]. Some LAB and bifidobacteria that possess β-glucosidase were proposed as a biotechnological resource in various fermented plant-based foods, as shown in Table 1.

2.1. Soymilk and Soybean Products

Isoflavones, which are produced almost exclusively by plants of the family Fabaceae, most often occur as glycosyl groups in plants. These compounds are found in plant sources mainly as O-glycosides, frequently bound to glucose, but also to other sugars such as galactose, rhamnose, arabinose, and xylose [102].
The biological activity of isoflavones has been well reported [103,104]. These compounds, known as phytoestrogens, are known to reduce the incidence of hormone-dependent steroid cancers such as breast, prostate, and colon cancer [105]. In addition, isoflavones have been shown to help prevent and treat several aging-related dysfunctions and diseases, including neurodegenerative disorders, osteoporosis, metabolic and cardiovascular diseases, and menopausal symptoms [106].
Soybeans (Glycine max) are important polyphenol sources in the diet because of their high levels of isoflavones [107]. Major isoflavones in soybean consist of three aglycones (daidzein, glycitein, and genistein) and their β-glycosides (daidzin, glycitin, and genistin), and acetyl and malonyl-conjugated β-glycosides (6″-O-acetyl daidzin, acetyl glycitin, and acetyl genistin; 6″O-malonyl daidzin, malonyl glycitin, and malonyl genistin) [108]. The O-β-glycosidic bonds of isoflavones are partially hydrolyzed in the gut primarily by microbial β-glycosidases to their aglycones, daidzein, genistein, and glycitein (Figure 2). Glucoside isoflavones are very poorly absorbed in the small intestine as compared with their aglycones, because of their greater molecular weight and higher hydrophilicity of the glucosides [109,110]. Furthermore, the isoflavone glucosides are known to be less bioactive than their respective aglycones [111].
Several studies have demonstrated that the content of aglycones in soy products was increased after microbial fermentation by LAB, which may be due to the changes of β-glucosidase activity [112,113,114]. Therefore, the use of these bacteria as starters, with the aforementioned enzymatic activity, in soy milk fermentation could contribute to increasing bioavailable isoflavones [115,116], thereby increasing the nutritional values and health benefits of fermented soy products [106].
Aglycones’ release is due to β-glucosidase activity on β-glucosides, which in most cases are also present as malonylated and acetylated forms. In these latter cases, β-glucosidase is part of a two-step process, which also requires an esterase enzyme to remove acetylation (Figure 2).
It has been shown that L. plantarum LP 95 was able to efficiently bio-transform glycosides to their bioactive aglycones, which could thus be used as a functional starter culture to increase the antioxidant activity of the fermented soymilk products [37,81]. Other studies have confirmed that several L. plantarum strains have great potential to enrich bioactive isoflavones in fermented soy milk products [115,117,118,119]. In recent studies, it has been shown that soy milk fermented from L. plantarum 200655 and L. plantarum KU210152 can be used as a prophylactic functional food with neuroprotective effects against oxidative stress [120,121]. Consistently, another study highlighted the increased antioxidant capacity of the L. plantarum-Y16-fermented soybean milk, with respect to an unfermented one, whose ethanol and water extracts were able to protect HepG2 cells against ABAP oxidative damage; this was reported to be dependent on the activation of the Nrf2/Keap1 signaling pathway and the upregulation of the expression of antioxidant systems such as heme oxygenase-1, superoxide dismutase, catalase, and glutathione peroxidase [122].
Therefore, increased availability of aglycones found in soy milk fermented with L. plantarum may be useful for designing new functional foods.
Moreover, use of selected L. plantarum strains which are more effective in increasing product bioactivity can also significantly increase the quality of a soy-waste product as okara. Ultrasonic treatment of L. plantarum BCRC 10357 was applied to induce a biological stress response resulting in a 100% increase in β-glucosidase activity, with this later responsible for the biotransformation of isoflavone glycosides to bioactive aglycones (daidzein and genistein) in okara [123]. In addition, the fermentation of enzymatically hydrolyzed okara by a L. plantarum UFG169 strain was reported to increase the content of both aglycone isoflavones and vitamin B2, as well as a reduction in off-flavors, thus improving both the nutrition and digestibility of this product [124].

2.2. Cassava

Cassava (Manihot esculenta Crantz), also known as yucca, manioc, or mandioca, is a perennial and herbaceous shrub that belongs to the class Malpighiales and Family Euphorbiceae. This crop has great social value and cultural identity, and it is now extensively cultivated throughout tropical and subtropical regions, mainly for its edible tubers as a source of carbohydrates, flavonoids, fiber, vitamin C, and minerals [125,126,127,128].
According to the Food and Agriculture Organization (FAO), cassava ranks fourth as a food crop in the developing countries, after rice, maize, and wheat [129]. Despite the advantages coming from its starchy tubers, other organs of cassava plant, such as leaves, can be also used for edible purposes. However, these less notable parts are characterized by a low protein content, rapid post-harvest deterioration, and the presence of cyanogenic glucosides, which are seen as major drawbacks which strongly limit its utilization as a food [130].
Consumption of improperly processed cassava may constitute a health problem in rural areas of sub-Saharan African countries where cassava-derived products provide a high percentage of the daily calory intake [131]. In severe cases, this may result in acute cyanide intoxication and in chronic paralytic diseases such as konzo and neurological disorders [132,133]. Moreover, cyanogenic glucosides are spread in all parts of the cassava plant, with the highest amounts in the leaves and the root cortex (skin layer) and are present in bound form, mostly 2-(β-D-glucopyranosyloxyl)isobutyronitrile (linamarin) and, to a lesser extent, its derivative 2-(β-D-glucopyranosyloxyl)methylbutyronitrile (lotaustralin) (Figure 3) [134].
These cyanogenic glucosides are not toxic as such because they are absorbed in the gastrointestinal tract and eliminated as such through urination. However, cyanogenic glycosides are hydrolyzed into acetone cyanohydrin by the glycosidases of gut microbiota. The acetone cyanohydrin was degraded spontaneously in the small intestine in which it had alkaline pH conditions. This degradation releases hydrocyanic acid (HCN), which bound to methemoglobin (Figure 3) [135,136] and, as known, exerts its toxicity by inhibiting the cytochrome oxidase, the complex IV of mitochondrial respiratory chain, thus preventing cellular utilization of oxygen [137]. The presence of these cyanogenic glucosides is the major limiting factor to direct utilization, thereby necessitating its processing prior to consumption. The introduction of new processing methods has helped to reduce cassava’s cyanogenic content and, therefore, exposure levels to its cyanogenic compounds. Cassava is traditionally processed by a wide range of methods, such as boiling, roasting, drying, cold water leaching, or fermentation [127], which reduce its toxicity. Thus, during fermentation, the roots are softened, and there is a disintegration of the tissue structure which causes linamarin to come into contact with endogenous linamerase, which is found in the cell wall, and microbial linamerase. These enzymatic activities result in subsequent hydrolysis into glucose and acetone cyanohydrin which are easily broken down into acetone and HCN. During the natural drying phase, free HCN evaporates easily by having a boiling point of 26 °C.
However, in spontaneous cassava fermentation, the activity of β-glycosidase is often not sufficient to break down all cyanogenic glycosides [138]. Moreover, the linamarase elaborated by both cassava plant tissues and fermenting microorganisms has been found to be unstable under the high acidic conditions characteristic of the latter part of natural fermentation. Therefore, it is important to review the detoxification methods of cassava and improve their effectiveness for greater consumption of cassava-based foods [139].
The cassava fermentation process can be carried out naturally (spontaneous fermentation) by relying on the native microbial populations present in the raw materials and in the environment.
However, the wide range and complexity of the microbiota of spontaneous cassava fermentation are the main factors responsible for the lack of homogeneity and low product quality [140]. The use of exogenous β-glucosidases from microbial sources is suggested, which hydrolyze these cyanogenic glycosides at an elevated level [141,142].
L. plantarum and other lactic acid bacteria (LAB) have been reported as the prevalent microorganisms associated with the spontaneous fermentation of cassava [128,143,144,145,146,147,148,149,150]. Some studies have shown that it is possible to significantly degrade cyanogenic glycosides and reduce free HCN in cassava through fermentation using L. plantarum as a single starter or in co-culture with other microorganisms [99,101,140,150,151,152,153,154,155].
Therefore, further studies are desirable for the establishment of new starter cultures that can contribute to the standardization of cassava fermentation conditions, thus ensuring higher quality products and consumer acceptability.
Especially, the selection and use of L. plantarum as a starter may be an effective biotechnological strategy that may allow for greater preservation, flavor enhancement, cyanide reduction, and improved functional properties of fermented cassava-based products [127].

2.3. Olive

Another emerging field of interest for L. plantarum β-glucosidases application is represented by olive production. One of the main problems of the olive industry, in fact, is the bitterness of olives which is principally due to the main representative of olive polyphenol glucosides, namely oleuropein [156]. Oleuropein is an O-glycosylated compound constituted by a D-glucose β (1-4) bound to aglycone, which can be hydrolyzed by the β-glucosidase enzyme resulting in D-glucose and aglycone production [157]. At present, the widely used method to debitter olive consists in the alkalyne treatment of drupes by means of NaOH solution; however, this method poses a series of concerns related to both the consumers (treatment-dependent reduction in nutrients) and the environment (wastewaters entrenched in toxic NaOH) [158]. At the same time, the olive debittering represents a committed step in the production of table olives giving rise to the search for alternative NaOH-free methods [159]; in this regard, the activity of microbial β-glucosidases proved to be able to hydrolyze oleuropein, thus producing low-molecular-weight phenolic compounds such as hydroxytyrosol and tyrosol [85,160]. Moreover, several papers showed the capability of L. plantarum to hydrolyze oleuropein, as well as the occurrence of this microorganism among the spontaneously fermenting species of table olives [45,161,162]. For these reasons, several strains of L. plantarum have been proposed as microbial cultures for table olive fermentation, since their adaptability to fermentation conditions, as well as high β-glucosidase activity makes this species particularly useful in olive debittering [87,163,164,165,166]. More recently, an elegant study [167] proposed three different mechanisms for the conversion of oleuropein into the active compound hydroxytyrosol, which seems to depend on the L. plantarum strain and need, besides β-glucosidases, and also the action of esterase activities.
In addition to olive debittering, L. plantarum fermentation has been suggested as a potential approach also for the recovery of valuable bioactive compounds, as hydroxytyrosol and tyrosol, from olive mill wastewater. This species, in fact, shares with the yest Wickerhamomyces anomalus the ability to increase the content of hydroxytyrosol in wastewater phenolic extract, with both microorganisms proving to be more efficient than the commercial enzyme in 2 h bioconversion tests [168]. In addition, a very recent study showed other functional properties of L. plantarum present in olive mill wastewater, such as the notable acidification capability and the production of antibacterial compounds [169]. These results provide strong evidence in making this species a candidate and its β-glucosidase activity as a powerful tool in the management of waste and by-products from the olive industry.

3. Fermented Beverages

3.1. Alcoholic Beverages

3.1.1. Wine

The wine LAB, naturally present in grape juice, play a significant role in winemaking by guiding a biological process known as malolactic fermentation (MLF).
This process involves the conversion of L-malic acid to L-lactic acid via malate decarboxylase, resulting in a reduction in wine acidity, providing microbiological stabilization and modifications of wine aroma [170].
In the last decades, various papers have shown that LAB metabolism also involves a large array of secondary enzymatic activities capable of generating many volatile secondary compounds as reviewed by Virdis and collaborators [171]. Many studies have shown that some non-Saccharomyces yeasts with high β-glucosidase activity play a vital role in improving the aroma complexity of wines by releasing aroma compounds from glycosidic precursors during fermentation [31,32,33]. However, several studies have demonstrated the presence of β-glycosidase activity in wine LAB, leading to the release of free volatile compounds as terpenes [172,173].
Oenococcus oeni is the main bacterial species responsible for malolactic fermentation; however, in the last two decades, it has been highlighted that other LAB associated with MLF have enormous potential to influence the composition of wine [171,174].
Among all the species, L. plantarum is frequently found on grapes and in wine and is considered as a new generation of MLF starter due to its ability of high ethanol tolerance and good enological characteristics [44,175,176,177,178,179,180,181,182,183]. In addition, L. plantarum has a wide range of enzymes, including β-glucosidase, which can also contribute significantly to the formation of wine aroma during the winemaking process [33,55,94,184].
It is because of these characteristics that some commercial starters belonging to L. plantarum species have been released in the last decade [185].
The hydrolysis of glycosides, previously reported during the malolactic fermentation through selected L. plantarum strains, may be considered as an interesting option to improve the sensorial characteristics of the wines.
Iorizzo et al. highlighted that some L. plantarum strains, candidates for MLF, were able to release specific terpenes from odourless grape glycosidic precursors [94]. In another study, L. plantarum M10, used as a malolactic starter after the alcoholic fermentation of Fiano grape juice, caused a significantly higher concentration of linalool in the wine [183].
Other authors found a significant increase in β-citronellol and 2-phenylethyl alcohol amounts after MLF with L. plantarum UNQLp 11 [186]. β-Citronellol is an alcoholic monoterpene that is most abundant in musts and wines and is often found as an odourless glyco-conjugated compound [65]. In addition, it has been hypothesized that β-glucosidase activity could also explain the increase in 2-phenylethyl alcohol (an aromatic alcohol that contributes to sweet floral attributes) in wine fermented with UNQLp 11, as previously described for other LAB strains [88].
In another study, the β-glucosidase activity of L. plantarum USC1 was stable between pH 4.5 and 7.5 and with a maximum activity at pH 5.0 and was completely inactivated at pH values below 4.0. The optimum temperature was 45 °C, and the enzyme was active against a wide range of aryl b-glucosides and b-linked disaccharides [187].
Brizuela et al. analyzed the amount of 1-octanol (mg/mL) obtained by the hydrolysis of the precursor octyl β-D-glucopyranoside in sterile Pinot Noir wine containing 14.5% v/v of ethanol, at different pH values (3.2, 3.5, and 3.8); the results of this study showed that the activity of β-glucosidase is reduced at low pH, but induced in the presence of high ethanol content [188].
Several studies have demonstrated that the β-glucosidase activity is mainly affected by pH, temperature, ethanol, and sugars [189,190,191,192].
Therefore, screening of L. plantarum strains for their glycosidase activities is important and should be performed based on the substrate to be fermented [88,193,194,195].

3.1.2. Beer

Sour beer is traditionally produced through spontaneous fermentations, involving complex microbial consortia, and is characterized by higher concentrations of organic acids. While the production of conventional beer is usually limited to yeast fermentation, the traditional production methods for sour beer, such as Lambic and Geuze beers, originating from Belgium, involve a spontaneous fermentation by multiple microorganisms, including yeasts and bacteria [196,197,198,199,200].
Interest in sour beer has increased substantially in recent decades, and research is underway on both spontaneous fermentations and alternative production techniques [201]. Pure-culture fermentations with strains of L. plantarum and Saccharomyces cerevisiae, in conjunction with the careful application of processing steps, offer a valid alternative to facilitate the production of sour beer. This approach provides a higher level of process control and more rapid fermentation compared to traditional methods [202,203,204].
The phenolic compounds found in wort and beer, especially phenolic acids and flavonoids, are derived mainly from barley malt and hops and are often present as glycosides [205]. The β-glucosidase activity promotes the bioavailability of these compounds by releasing the aglycones. These phenolic compounds have several functional properties in beer, influencing its colloidal stability, flavor, color, and after deglycosylation increase some beneficial biological effects on human health [206,207,208].
In a recent study, the co-inoculation of L. plantarum CECT 9567 and S. cerevisiae was applied for the production of a probiotic beer [209]. The authors attribute the higher polyphenol content observed in beers brewed with co-inoculation to two phenomena: hydrolysis of bound polyphenols and increased free polyphenols. These phenomena are significantly related to β-glucosidase activity [210,211].

3.2. Non-Alcoholic Fermented Fruit Products

Plant-based foods, including fruits and vegetables, are naturally rich in minerals, vitamins, dietary fibers, antioxidants, and many other beneficial nutrients that make them essential components of a healthy and balanced diet. Due to new healthy trends, consumption of fruit and vegetable juices have increased in recent years [212].
Two predominant fermentation pathways have been identified in the production of fruit juices: the alcoholic pathway, which involves the utilization of yeast, and the non-alcoholic pathway, which relies on the action of LAB.
Being a traditional food biotechnology, fermentation by LAB is widely used for fruit and vegetable fermentation to convert bioactive components, enhance beneficial properties, extend shelf-life, and improve sensory characteristics of final products [213,214].
Fermentation by LAB increases the content of functional nutrients, including polyphenols, flavonoids, organic acids, polysaccharides, amino acids, vitamins, minerals, and other efficacious components, giving the fruit excellent antioxidant, antibacterial, anti-inflammatory, and gut microbiota modulation activities [215,216,217].
Moreover, LAB fermentation can impart distinctive fruity and floral aromas to fruits through the production of esters, ketones, alcohols, terpenes, etc. [218,219,220].
Among the LAB, L. plantarum is quite interesting, as far as its application in the fermentation of a wide range of plant-based substrates is concerned, such as vegetables and fruit juices, since it has genome plasticity and high versatility and flexibility [213].
Several studies have shown that L. plantarum, used as a starter culture, facilitates the enhancement of flavor and aroma in fermented fruit juices through its β-glucosidase activity. Pomegranate juices fermented by L. plantarum POM1 and LP09 were characterized by high levels of terpenes, such as limonene, β-myrcene, γ-terpinene, α-terpinene, α-terpinolene, and p-cymene [97]. Monoterpenes are present in pomegranate juice as either free or glycosidically conjugated precursors and the release of glycosidically bound aromatic compounds has been shown to result in the modification or enhancement of its characteristic flavor [221]. It has been found that Sabre mango juice fermented with L. plantarum L75 produced higher levels of β-myrcene [222]. A similar increase in β-myrcene was reported in L. plantarum POM1- and LP09-fermented pomegranate juices [97].
In addition to the flavor properties, several biological activities were recognized from β-myrcene as having anxiolytic, antioxidant, anti-aging, anti-inflammatory, and analgesic effects in mammals [223], as well as toxicity against pest [224].
A recent study showed that the nutritional quality and flavor characteristics of apricot juice can be improved by L. plantarum LP56 fermentation; specifically, after 6 h, there was a significant increase in the content of volatile compounds, including α-terpineol, nerol, β-pinene, and terpinene, reaching its maximum level [225].
Myrtenol is a volatile compound belonging to the terpenoid family of monocyclic monoterpenes and contributed to the woody, pine, balsam, sweet, and mint notes. In addition, several reports demonstrated the pharmacological properties of myrtenol, including its antioxidant, antibacterial, antifungal, antidiabetic, anxiolytic, and gastroprotective activities [226]. Fermentation of Momordica charantia juice by L. plantarum NCU116 improved its aroma profile, with myrthenol as the main aromatic compound, and resulted in a beneficial effect on the physicochemical properties, bioactive compounds, and antioxidant property of the juice [227].
Ricci et al. detected, among the terpene and norisoprenoid class, an increase in limonene, β-linalool, β-damascenon, and eugenol in elderberry juice fermented by L. plantarum 285 [228].
The increase in these compounds could be related to the ability of L. plantarum to produce β-glucosidase [94,97,219].
Fruit beverages fermented by L. plantarum, not only are characterized by a pleasant aroma and taste, but show many health-promoting benefits due to their content of metabolites such as vitamins, organic acids, and phenolic compounds [229,230,231,232].
Several studies have shown that the bioavailability of phenolic compounds is enhanced by different LAB after fermentation of different fruit products [218,233,234,235].
According to several studies, L. plantarum produces enzymes such as β-glucosidase during the fermentation process, which is able to hydrolyze phenolic glycosides to the corresponding aglycones, which have radical scavenging properties [211,236,237]. This process results in an increase in the antioxidant activity of the fermented product [238].
The antioxidant activity of phenolics is related to their chemical structure. In general, flavonoid compounds present a stronger antioxidant activity than non-flavonoids, and combined forms such as glycosides present a lower activity than the free forms [239].
In a study conducted by Meng et al. the effect of different L. plantarum strains on the physicochemical characteristics and antioxidant activities of loquat juice was investigated. Results showed that nerolidol production was significantly upregulated in loquat juices fermented by L. plantarum LP2 [240].
Nerolidol, a terpenoid has good anti-inflammatory, antioxidant, neuroprotective, and cardioprotective activities [241,242]. Furthermore, after fermentation by L. plantarum LP2 the antioxidant activity and the total flavonoid content in loquat juice significantly increased.
Landete et al. showed that deglycosylation by L. plantarum CECT 748 transformed food aryl glycosides (phloridzin, esculin, daidzin, and salicin) into their corresponding aryl aglycones (phloretin, esculetin, daidzein, and saligenin). Therefore, in addition to the improvement of their bioavailability, the deglycosylation of specific aryl glycosides by L. plantarum CECT 748 increase the antioxidant activity of glycosylated phenolic compounds [194]. Moreover, besides the aglycone release, the antioxidant activity in fermented foods can be modulated also by other mechanisms, as antioxidant enzymes, bioactive peptides, and exopolysaccharides produced by L. plantarum [243].
Table 2 shows the main positive effects of the enzymatic activity of L. plantarum, mainly attributable to β-glucosidase, in different fermented fruit products. The data refer to articles published in the last 10 years. However, the impact of fermentation on phenolic compounds seems to depend heavily on the bacterial strain used and the starting material.
Li et al. reported that LAB fermentation with L. plantarum 90 significantly increased the total phenolic content, while decreasing the total flavonoid content in fermented jujube juices [254].
The same author had found that the fermentation of apple juice by L. plantarum ATCC14917 caused an increase in antioxidant activity while decreasing the total content of phenols and flavonoids [244], attributing to, according to Tian, the greater antioxidant captivity detected in other possible mechanisms [267].
In another study, the flavonol glycosides in sea buckthorn as well as anthocyanins in chokeberry remained unaffected by the fermentation with several L. plantarum strains obtained from DSMZ (Braunschweig, Germany) [268].
Wei et al. [269] reported a general decrease in anthocyanins, phenolic acids, flavonols, and flavanols in bog bilberry juice fermented with L. plantarum B7 or L. plantarum C8-1.
Therefore, this suggests that careful selection within the L. plantarum species is crucial in order to identify the most suitable strains to be used for each specific biotechnological application aimed at improving the functional properties of the final products [270].

4. Conclusions

In the last decades, the needs of both producers and consumers in the food sector have continuously grown, thus requiring a particular attention not only to organoleptic aspects but also in terms of health and well-being. This review shows how the enzyme β-glucosidase can be considered crucial for the hydrolysis of several glycosides that give added value to the fermented food matrix. In particular, the activity of β-glucosidase during fermentation by L. plantarum can be considered an important biotechnological strategy in order to increase the nutritional, sensory, and functional properties of specific fermented foods. The studies cited in this review showed that the optimal conditions for the β-glucosidase activity differs extensively among the L. plantarum strains and is significantly affected by substrate composition and culture conditions. Therefore, it is essential to optimize these conditions to improve this enzymatic activity and also, according to the production process adopted, to obtain each specific fermented food. Considering that lactic fermentation is an important technology to increase functional properties of fermented foods, we believe that the selection of β-glucosidase-producing L. plantarum strains should remain a focal point of interest in future research, since it can be a valid tool for the design of new functional foods.

Author Contributions

Conceptualization, M.I., C.D.M. and G.P.; writing—original draft preparation, M.I. and G.P.; writing—review and editing, M.I., G.P., C.D.M. and F.C.; visualization, C.D.M.; supervision, M.I. All authors have read and agreed to the published version of the manuscript.

Funding

This research received no external funding.

Institutional Review Board Statement

Not applicable.

Informed Consent Statement

Not applicable.

Data Availability Statement

The original contributions presented in the study are included in the article, and further inquiries can be directed to the corresponding author.

Conflicts of Interest

The authors declare no conflicts of interest.

References

  1. Sengupta, S.; Datta, M.; Datta, S. β-Glucosidase: Structure, Function and Industrial Applications. In Glycoside Hydrolases; Elsevier: Amsterdam, The Netherlands, 2023; pp. 97–120. [Google Scholar]
  2. Shen, H.; Byers, L.D. Thioglycoside Hydrolysis Catalyzed by β-Glucosidase. Biochem. Biophys. Res. Commun. 2007, 362, 717–720. [Google Scholar] [CrossRef] [PubMed]
  3. Henrissat, B. A Classification of Glycosyl Hydrolases Based on Amino Acid Sequence Similarities. Biochem. J. 1991, 280, 309–316. [Google Scholar] [CrossRef]
  4. Henrissat, B.; Davies, G. Structural and Sequence-Based Classification of Glycoside Hydrolases. Curr. Opin. Struct. Biol. 1997, 7, 637–644. [Google Scholar] [CrossRef]
  5. Ketudat Cairns, J.R.; Esen, A. β-Glucosidases. Cell. Mol. Life Sci. 2010, 67, 3389–3405. [Google Scholar] [CrossRef] [PubMed]
  6. Cantarel, B.L.; Coutinho, P.M.; Rancurel, C.; Bernard, T.; Lombard, V.; Henrissat, B. The Carbohydrate-Active EnZymes Database (CAZy): An Expert Resource for Glycogenomics. Nucleic Acids Res. 2009, 37, D233–D238. [Google Scholar] [CrossRef]
  7. Kannan, P.; Shafreen, M.M.; Achudhan, A.B.; Gupta, A.; Saleena, L.M. A Review on Applications of β-Glucosidase in Food, Brewery, Pharmaceutical and Cosmetic Industries. Carbohydr. Res. 2023, 530, 108855. [Google Scholar] [CrossRef]
  8. Magwaza, B.; Amobonye, A.; Pillai, S. Microbial β-Glucosidases: Recent Advances and Applications. Biochimie 2024, 225, 49–67. [Google Scholar] [CrossRef]
  9. Mól, P.C.G.; Júnior, J.C.Q.; Veríssimo, L.A.A.; Boscolo, M.; Gomes, E.; Minim, L.A.; Da Silva, R. β-Glucosidase: An Overview on Immobilization and Some Aspects of Structure, Function, Applications and Cost. Process Biochem. 2023, 130, 26–39. [Google Scholar] [CrossRef]
  10. Singh, G.; Verma, A.K.; Kumar, V. Catalytic Properties, Functional Attributes and Industrial Applications of β-Glucosidases. 3 Biotech. 2016, 6, 3. [Google Scholar] [CrossRef]
  11. Ouyang, B.; Wang, G.; Zhang, N.; Zuo, J.; Huang, Y.; Zhao, X. Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review. Molecules 2023, 28, 4990. [Google Scholar] [CrossRef]
  12. Liu, C.; He, S.; Chen, J.; Wang, M.; Li, Z.; Wei, L.; Chen, Y.; Du, M.; Liu, D.; Li, C.; et al. A Dual-subcellular Localized Β-glucosidase Confers Pathogen and Insect Resistance without a Yield Penalty in Maize. Plant Biotechnol. J. 2024, 22, 1017–1032. [Google Scholar] [CrossRef]
  13. Kotik, M.; Kulik, N.; Valentová, K. Flavonoids as Aglycones in Retaining Glycosidase-Catalyzed Reactions: Prospects for Green Chemistry. J. Agric. Food Chem. 2023, 71, 14890–14910. [Google Scholar] [CrossRef] [PubMed]
  14. Xu, P.; Wu, T.; Ali, A.; Wang, J.; Fang, Y.; Qiang, R.; Liu, Y.; Tian, Y.; Liu, S.; Zhang, H.; et al. Rice β-Glucosidase 4 (Os1βGlu4) Regulates the Hull Pigmentation via Accumulation of Salicylic Acid. Int. J. Mol. Sci. 2022, 23, 10646. [Google Scholar] [CrossRef]
  15. Lee, K.H.; Piao, H.L.; Kim, H.-Y.; Choi, S.M.; Jiang, F.; Hartung, W.; Hwang, I.; Kwak, J.M.; Lee, I.-J.; Hwang, I. Activation of Glucosidase via Stress-Induced Polymerization Rapidly Increases Active Pools of Abscisic Acid. Cell 2006, 126, 1109–1120. [Google Scholar] [CrossRef]
  16. Sakr, S.; Wang, M.; Dédaldéchamp, F.; Perez-Garcia, M.-D.; Ogé, L.; Hamama, L.; Atanassova, R. The Sugar-Signaling Hub: Overview of Regulators and Interaction with the Hormonal and Metabolic Network. Int. J. Mol. Sci. 2018, 19, 2506. [Google Scholar] [CrossRef] [PubMed]
  17. Boer, D.E.C.; van Smeden, J.; Bouwstra, J.A.; Aerts, J.M.F.G. Glucocerebrosidase: Functions in and Beyond the Lysosome. J. Clin. Med. 2020, 9, 736. [Google Scholar] [CrossRef] [PubMed]
  18. Day, A.J.; Cañada, F.J.; Díaz, J.C.; Kroon, P.A.; Mclauchlan, R.; Faulds, C.B.; Plumb, G.W.; Morgan, M.R.A.; Williamson, G. Dietary Flavonoid and Isoflavone Glycosides Are Hydrolysed by the Lactase Site of Lactase Phlorizin Hydrolase. FEBS Lett. 2000, 468, 166–170. [Google Scholar] [CrossRef]
  19. Elferink, H.; Bruekers, J.P.J.; Veeneman, G.H.; Boltje, T.J. A Comprehensive Overview of Substrate Specificity of Glycoside Hydrolases and Transporters in the Small Intestine. Cell. Mol. Life Sci. 2020, 77, 4799–4826. [Google Scholar] [CrossRef]
  20. He, S.; Jiang, B.; Chakraborty, A.; Yu, G. The Evolution of Glycoside Hydrolase Family 1 in Insects Related to Their Adaptation to Plant Utilization. Insects 2022, 13, 786. [Google Scholar] [CrossRef]
  21. Friedrichs, J.; Schweiger, R.; Müller, C. Unique Metabolism of Different Glucosinolates in Larvae and Adults of a Leaf Beetle Specialised on Brassicaceae. Sci. Rep. 2022, 12, 10905. [Google Scholar] [CrossRef]
  22. Bhatia, Y.; Mishra, S.; Bisaria, V.S. Microbial β-Glucosidases: Cloning, Properties, and Applications. Crit. Rev. Biotechnol. 2002, 22, 375–407. [Google Scholar] [CrossRef] [PubMed]
  23. Fu, Y.; Yin, Z.; Wu, L.; Yin, C. Diversity of Cultivable β-Glycosidase-Producing Micro-Organisms Isolated from the Soil of a Ginseng Field and Their Ginsenosides-Hydrolysing Activity. Lett. Appl. Microbiol. 2014, 58, 138–144. [Google Scholar] [CrossRef]
  24. Tiwari, R.; Kumar, K.; Singh, S.; Nain, L.; Shukla, P. Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats. Front. Microbiol. 2016, 7, 1597. [Google Scholar] [CrossRef]
  25. Su, H.; Xiao, Z.; Yu, K.; Zhang, Q.; Lu, C.; Wang, G.; Wang, Y.; Liang, J.; Huang, W.; Huang, X.; et al. High Diversity of β-Glucosidase-Producing Bacteria and Their Genes Associated with Scleractinian Corals. Int. J. Mol. Sci. 2021, 22, 3523. [Google Scholar] [CrossRef] [PubMed]
  26. Oladoja, E.; Oyewole, O.; Adamu, B.; Balogun, A.; Musa, O. Microbial β-Glucosidase: Source, Production and Applications. Int. J. Biol. Sci. 2019, 1, 14–22. [Google Scholar] [CrossRef]
  27. Zang, X.; Liu, M.; Fan, Y.; Xu, J.; Xu, X.; Li, H. The Structural and Functional Contributions of β-Glucosidase-Producing Microbial Communities to Cellulose Degradation in Composting. Biotechnol. Biofuels 2018, 11, 51. [Google Scholar] [CrossRef] [PubMed]
  28. Ahmed, A.; Nasim, F.; Batool, K.; Bibi, A. Microbial β-Glucosidase: Sources, Production and Applicationsc. J. Appl. Environ. Microbiol. 2017, 5, 31–46. [Google Scholar] [CrossRef]
  29. Yang, W.; Su, Y.; Wang, R.; Zhang, H.; Jing, H.; Meng, J.; Zhang, G.; Huang, L.; Guo, L.; Wang, J.; et al. Microbial Production and Applications of β-Glucosidase-A Review. Int. J. Biol. Macromol. 2024, 256, 127915. [Google Scholar] [CrossRef]
  30. Michlmayr, H.; Kneifel, W. β-Glucosidase Activities of Lactic Acid Bacteria: Mechanisms, Impact on Fermented Food and Human Health. FEMS Microbiol. Lett. 2014, 352, 1–10. [Google Scholar] [CrossRef]
  31. Gao, P.; Peng, S.; Sam, F.E.; Zhu, Y.; Liang, L.; Li, M.; Wang, J. Indigenous Non-Saccharomyces Yeasts with β-Glucosidase Activity in Sequential Fermentation with Saccharomyces Cerevisiae: A Strategy to Improve the Volatile Composition and Sensory Characteristics of Wines. Front. Microbiol. 2022, 13, 845837. [Google Scholar] [CrossRef]
  32. Testa, B.; Lombardi, S.J.; Iorizzo, M.; Letizia, F.; Di Martino, C.; Di Renzo, M.; Strollo, D.; Tremonte, P.; Pannella, G.; Ianiro, M.; et al. Use of Strain Hanseniaspora Guilliermondii BF1 for Winemaking Process of White Grapes Vitis vinifera Cv Fiano. Eur. Food Res. Technol. 2020, 246, 549–561. [Google Scholar] [CrossRef]
  33. Testa, B.; Coppola, F.; Iorizzo, M.; Di Renzo, M.; Coppola, R.; Succi, M. Preliminary Characterisation of Metschnikowia Pulcherrima to Be Used as a Starter Culture in Red Winemaking. Beverages 2024, 10, 88. [Google Scholar] [CrossRef]
  34. Colautti, A.; Camprini, L.; Ginaldi, F.; Comi, G.; Reale, A.; Coppola, F.; Iacumin, L. Safety Traits, Genetic and Technological Characterization of Lacticaseibacillus Rhamnosus Strains. LWT 2024, 207, 116578. [Google Scholar] [CrossRef]
  35. Coppola, F.; Abdalrazeq, M.; Fratianni, F.; Ombra, M.N.; Testa, B.; Zengin, G.; Ayala Zavala, J.F.; Nazzaro, F. Rosaceae Honey: Antimicrobial Activity and Prebiotic Properties. Antibiotics 2025, 14, 298. [Google Scholar] [CrossRef]
  36. Nazzaro, F.; Ombra, M.N.; Coppola, F.; De Giulio, B.; d’Acierno, A.; Coppola, R.; Fratianni, F. Antibacterial Activity and Prebiotic Properties of Six Types of Lamiaceae Honey. Antibiotics 2024, 13, 868. [Google Scholar] [CrossRef]
  37. Letizia, F.; Fusco, G.M.; Fratianni, A.; Gaeta, I.; Carillo, P.; Messia, M.C.; Iorizzo, M. Application of Lactiplantibacillus plantarum LP95 as a Functional Starter Culture in Fermented Tofu Production. Processes 2024, 12, 1093. [Google Scholar] [CrossRef]
  38. Berthiller, F.; Krska, R.; Domig, K.J.; Kneifel, W.; Juge, N.; Schuhmacher, R.; Adam, G. Hydrolytic Fate of Deoxynivalenol-3-Glucoside during Digestion. Toxicol. Lett. 2011, 206, 264–267. [Google Scholar] [CrossRef]
  39. Siezen, R.J.; Tzeneva, V.A.; Castioni, A.; Wels, M.; Phan, H.T.K.; Rademaker, J.L.W.; Starrenburg, M.J.C.; Kleerebezem, M.; Molenaar, D.; Van Hylckama Vlieg, J.E.T. Phenotypic and Genomic Diversity of Lactobacillus plantarum Strains Isolated from Various Environmental Niches. Environ. Microbiol. 2010, 12, 758–773. [Google Scholar] [CrossRef]
  40. Martino, M.E.; Bayjanov, J.R.; Caffrey, B.E.; Wels, M.; Joncour, P.; Hughes, S.; Gillet, B.; Kleerebezem, M.; van Hijum, S.A.F.T.; Leulier, F. Nomadic Lifestyle of Lactobacillus plantarum Revealed by Comparative Genomics of 54 Strains Isolated from Different Habitats. Environ. Microbiol. 2016, 18, 4974–4989. [Google Scholar] [CrossRef]
  41. Siezen, R.J.; van Hylckama Vlieg, J.E.T. Genomic Diversity and Versatility of Lactobacillus plantarum, a Natural Metabolic Engineer. Microb. Cell Fact. 2011, 10, S3. [Google Scholar] [CrossRef]
  42. Letizia, F.; Albanese, G.; Testa, B.; Vergalito, F.; Bagnoli, D.; Di Martino, C.; Carillo, P.; Verrillo, L.; Succi, M.; Sorrentino, E.; et al. In Vitro Assessment of Bio-Functional Properties from Lactiplantibacillus plantarum Strains. Curr. Issues Mol. Biol. 2022, 44, 2321–2334. [Google Scholar] [CrossRef]
  43. Filannino, P.; De Angelis, M.; Di Cagno, R.; Gozzi, G.; Riciputi, Y.; Gobbetti, M. How Lactobacillus plantarum Shapes Its Transcriptome in Response to Contrasting Habitats. Environ. Microbiol. 2018, 20, 3700–3716. [Google Scholar] [CrossRef]
  44. Testa, B.; Lombardi, S.J.; Tremonte, P.; Succi, M.; Tipaldi, L.; Pannella, G.; Sorrentino, E.; Iorizzo, M.; Coppola, R. Biodiversity of Lactobacillus plantarum from Traditional Italian Wines. World J. Microbiol. Biotechnol. 2014, 30, 2299–2305. [Google Scholar] [CrossRef] [PubMed]
  45. Iorizzo, M.; Lombardi, S.J.; Macciola, V.; Testa, B.; Lustrato, G.; Lopez, F.; De Leonardis, A. Technological Potential of Lactobacillus Strains Isolated from Fermented Green Olives: In Vitro Studies with Emphasis on Oleuropein-Degrading Capability. Sci. World J. 2016, 2016, 1917592. [Google Scholar] [CrossRef]
  46. Iorizzo, M.; Testa, B.; Ganassi, S.; Lombardi, S.J.; Ianiro, M.; Letizia, F.; Succi, M.; Tremonte, P.; Vergalito, F.; Cozzolino, A.; et al. Probiotic Properties and Potentiality of Lactiplantibacillus plantarum Strains for the Biological Control of Chalkbrood Disease. J. Fungi 2021, 7, 379. [Google Scholar] [CrossRef]
  47. Chundakkattumalayil, H.C.; Raghavan, K.T. Health Endorsing Potential of Lactobacillus plantarum MBTU-HK1 and MBTU-HT of Honey Bee Gut Origin. J. Appl. Biol. Biotechnol. 2021, 9, 63–68. [Google Scholar] [CrossRef]
  48. Iorizzo, M.; Pannella, G.; Lombardi, S.J.; Ganassi, S.; Testa, B.; Succi, M.; Sorrentino, E.; Petrarca, S.; De Cristofaro, A.; Coppola, R.; et al. Inter- and Intra-Species Diversity of Lactic Acid Bacteria in Apis mellifera ligustica Colonies. Microorganisms 2020, 8, 1578. [Google Scholar] [CrossRef]
  49. Iorizzo, M.; Albanese, G.; Testa, B.; Ianiro, M.; Letizia, F.; Succi, M.; Tremonte, P.; D’andrea, M.; Iaffaldano, N.; Coppola, R. Presence of Lactic Acid Bacteria in the Intestinal Tract of the Mediterranean Trout (Salmo macrostigma) in Its Natural Environment. Life 2021, 11, 667. [Google Scholar] [CrossRef]
  50. Park, S.-Y.; Lim, S.-D. Probiotic Characteristics of Lactobacillus plantarum FH185 Isolated from Human Feces. Korean J. Food Sci. Anim. Resour. 2015, 35, 615–621. [Google Scholar] [CrossRef] [PubMed]
  51. Salvetti, E.; O’Toole, P.W. When Regulation Challenges Innovation: The Case of the Genus Lactobacillus. Trends Food Sci. Technol. 2017, 66, 187–194. [Google Scholar] [CrossRef]
  52. Koutsoumanis, K.; Allende, A.; Alvarez-Ordóñez, A.; Bolton, D.; Bover-Cid, S.; Chemaly, M.; Davies, R.; De Cesare, A.; Hilbert, F.; Lindqvist, R.; et al. Update of the List of QPS-recommended Biological Agents Intentionally Added to Food or Feed as Notified to EFSA 12: Suitability of Taxonomic Units Notified to EFSA until March 2020. EFSA J. 2020, 18, e06174. [Google Scholar] [CrossRef] [PubMed]
  53. Iorizzo, M.; Paventi, G.; Di Martino, C. Biosynthesis of Gamma-Aminobutyric Acid (GABA) by Lactiplantibacillus plantarum in Fermented Food Production. Curr. Issues Mol. Biol. 2023, 46, 200–220. [Google Scholar] [CrossRef] [PubMed]
  54. Iorizzo, M.; Di Martino, C.; Letizia, F.; Crawford, T.W.; Paventi, G. Production of Conjugated Linoleic Acid (CLA) by Lactiplantibacillus plantarum: A Review with Emphasis on Fermented Foods. Foods 2024, 13, 975. [Google Scholar] [CrossRef]
  55. Paventi, G.; Di Martino, C.; Crawford, T.W., Jr.; Iorizzo, M. Enzymatic Activities of Lactiplantibacillus plantarum: Technological and Functional Role in Food Processing and Human Nutrition. Food Biosci. 2024, 61, 104944. [Google Scholar] [CrossRef]
  56. Behera, S.S.; Ray, R.C.; Zdolec, N. Lactobacillus plantarum with Functional Properties: An Approach to Increase Safety and Shelf-Life of Fermented Foods. BioMed Res. Int. 2018, 2018, 9361614. [Google Scholar] [CrossRef]
  57. Caffrey, A.J.; Lerno, L.A.; Zweigenbaum, J.; Ebeler, S.E. Direct Analysis of Glycosidic Aroma Precursors Containing Multiple Aglycone Classes in Vitis vinifera Berries. J. Agric. Food Chem. 2020, 68, 3817–3833. [Google Scholar] [CrossRef]
  58. Liang, Z.; Fang, Z.; Pai, A.; Luo, J.; Gan, R.; Gao, Y.; Lu, J.; Zhang, P. Glycosidically Bound Aroma Precursors in Fruits: A Comprehensive Review. Crit. Rev. Food Sci. Nutr. 2022, 62, 215–243. [Google Scholar] [CrossRef]
  59. Zhu, N.; Wang, T.; Ge, L.; Li, Y.; Zhang, X.; Bao, H. γ-Amino Butyric Acid (GABA) Synthesis Enabled by Copper-Catalyzed Carboamination of Alkenes. Org. Lett. 2017, 19, 4718–4721. [Google Scholar] [CrossRef]
  60. González-Barreiro, C.; Rial-Otero, R.; Cancho-Grande, B.; Simal-Gándara, J. Wine Aroma Compounds in Grapes: A Critical Review. Crit. Rev. Food Sci. Nutr. 2015, 55, 202–218. [Google Scholar] [CrossRef]
  61. Maicas, S.; Mateo, J.J. Hydrolysis of Terpenyl Glycosides in Grape Juice and Other Fruit Juices: A Review. Appl. Microbiol. Biotechnol. 2005, 67, 322–335. [Google Scholar] [CrossRef]
  62. Krammer, G.; Winterhalter, P.; Schwab, M.; Schreier, P. Glycosidically Bound Aroma Compounds in the Fruits of Prunus Species: Apricot (P. armeniaca, L.), Peach (P. persica, L.), Yellow Plum (P. domestica, L. ssp. syriaca). J. Agric. Food Chem. 1991, 39, 778–781. [Google Scholar] [CrossRef]
  63. de Morais Souto, B.; Florentino Barbosa, M.; Marinsek Sales, R.M.; Conessa Moura, S.; de Rezende Bastos Araújo, A.; Ferraz Quirino, B. The Potential of β-Glucosidases for Aroma and Flavor Improvement in the Food Industry. Microbe 2023, 1, 100004. [Google Scholar] [CrossRef]
  64. Fernández-Pacheco, P.; García-Béjar, B.; Briones Pérez, A.; Arévalo-Villena, M. Free and Immobilised β-Glucosidases in Oenology: Biotechnological Characterisation and Its Effect on Enhancement of Wine Aroma. Front. Microbiol. 2021, 12, 723815. [Google Scholar] [CrossRef] [PubMed]
  65. Sarry, J.; Gunata, Z. Plant and Microbial Glycoside Hydrolases: Volatile Release from Glycosidic Aroma Precursors. Food Chem. 2004, 87, 509–521. [Google Scholar] [CrossRef]
  66. Wang, Z.; Chen, K.; Liu, C.; Ma, L.; Li, J. Effects of Glycosidase on Glycoside-Bound Aroma Compounds in Grape and Cherry Juice. J. Food Sci. Technol. 2023, 60, 761–771. [Google Scholar] [CrossRef] [PubMed]
  67. Dziadas, M.; Jeleń, H.H. Comparison of Enzymatic and Acid Hydrolysis of Bound Flavor Compounds in Model System and Grapes. Food Chem. 2016, 190, 412–418. [Google Scholar] [CrossRef]
  68. Muradova, M.; Proskura, A.; Canon, F.; Aleksandrova, I.; Schwartz, M.; Heydel, J.-M.; Baranenko, D.; Nadtochii, L.; Neiers, F. Unlocking Flavor Potential Using Microbial β-Glucosidases in Food Processing. Foods 2023, 12, 4484. [Google Scholar] [CrossRef]
  69. Maicas, S.; Mateo, J. Microbial Glycosidases for Wine Production. Beverages 2016, 2, 20. [Google Scholar] [CrossRef]
  70. Hjelmeland, A.K.; Ebeler, S.E. Glycosidically Bound Volatile Aroma Compounds in Grapes and Wine: A Review. Am. J. Enol. Vitic. 2015, 66, 1–11. [Google Scholar] [CrossRef]
  71. Wilkowska, A.; Pogorzelski, E. Aroma Enhancement of Cherry Juice and Wine Using Exogenous Glycosidases from Mould, Yeast and Lactic Acid Bacteria. Food Chem. 2017, 237, 282–289. [Google Scholar] [CrossRef]
  72. Zhang, Z.; Li, X.; Sang, S.; McClements, D.J.; Chen, L.; Long, J.; Jiao, A.; Jin, Z.; Qiu, C. Polyphenols as Plant-Based Nutraceuticals: Health Effects, Encapsulation, Nano-Delivery, and Application. Foods 2022, 11, 2189. [Google Scholar] [CrossRef]
  73. Sun, H.; Xue, Y.; Lin, Y. Enhanced Catalytic Efficiency in Quercetin-4′-Glucoside Hydrolysis of Thermotoga maritima β-Glucosidase A by Site-Directed Mutagenesis. J. Agric. Food Chem. 2014, 62, 6763–6770. [Google Scholar] [CrossRef]
  74. Del Rio, D.; Rodriguez-Mateos, A.; Spencer, J.P.E.; Tognolini, M.; Borges, G.; Crozier, A. Dietary (Poly)Phenolics in Human Health: Structures, Bioavailability, and Evidence of Protective Effects against Chronic Diseases. Antioxid. Redox Signal. 2013, 18, 1818–1892. [Google Scholar] [CrossRef] [PubMed]
  75. Yang, X.; Hong, J.; Wang, L.; Cai, C.; Mo, H.; Wang, J.; Fang, X.; Liao, Z. Effect of Lactic Acid Bacteria Fermentation on Plant-Based Products. Fermentation 2024, 10, 48. [Google Scholar] [CrossRef]
  76. Niamah, A.K.; Al-fekaiki, D.F.; Thyab Gddoa Al-Sahlany, S.; Verma, D.K.; Patel, A.R.; Singh, S. Investigating the Effect of Addition of Probiotic Microorganisms (Bacteria or Yeast) to Yoghurt on the Viability and Volatile Aromatic Profiles. J. Food Meas. Charact. 2023, 17, 5463–5473. [Google Scholar] [CrossRef]
  77. Gaya, P.; Peirotén, Á.; Landete, J.M. Expression of a β-Glucosidase in Bacteria with Biotechnological Interest Confers Them the Ability to Deglycosylate Lignans and Flavonoids in Vegetal Foods. Appl. Microbiol. Biotechnol. 2020, 104, 4903–4913. [Google Scholar] [CrossRef] [PubMed]
  78. Delgado, S.; Guadamuro, L.; Flórez, A.B.; Vázquez, L.; Mayo, B. Fermentation of Commercial Soy Beverages with Lactobacilli and Bifidobacteria Strains Featuring High β-Glucosidase Activity. Innov. Food Sci. Emerg. Technol. 2019, 51, 148–155. [Google Scholar] [CrossRef]
  79. Hati, S.; Vij, S.; Singh, B.P.; Mandal, S. β-Glucosidase Activity and Bioconversion of Isoflavones during Fermentation of Soymilk. J. Sci. Food Agric. 2015, 95, 216–220. [Google Scholar] [CrossRef]
  80. de Oliveira Galdino, I.K.C.P.; da Silva, M.O.M.; da Silva, A.P.A.; Santos, V.N.; Feitosa, R.L.P.; Ferreira, L.C.N.; Dantas, G.C.; dos Santos Pereira, E.V.; de Oliveira, T.A.; dos Santos, K.M.O.; et al. β-Glucosidase Activity and Antimicrobial Properties of Potentially Probiotic Autochthonous Lactic Cultures. PeerJ 2023, 11, e16094. [Google Scholar] [CrossRef]
  81. Letizia, F.; Fratianni, A.; Cofelice, M.; Testa, B.; Albanese, G.; Di Martino, C.; Panfili, G.; Lopez, F.; Iorizzo, M. Antioxidative Properties of Fermented Soymilk Using Lactiplantibacillus plantarum LP95. Antioxidants 2023, 12, 1442. [Google Scholar] [CrossRef]
  82. Son, S.-H.; Jeon, H.-L.; Yang, S.-J.; Sim, M.-H.; Kim, Y.-J.; Lee, N.-K.; Paik, H.-D. Probiotic Lactic Acid Bacteria Isolated from Traditional Korean Fermented Foods Based on β-Glucosidase Activity. Food Sci. Biotechnol. 2018, 27, 123–129. [Google Scholar] [CrossRef]
  83. Santos, M.M.; Piccirillo, C.; Castro, P.M.L.; Kalogerakis, N.; Pintado, M.E. Bioconversion of Oleuropein to Hydroxytyrosol by Lactic Acid Bacteria. World J. Microbiol. Biotechnol. 2012, 28, 2435–2440. [Google Scholar] [CrossRef]
  84. Landete, J.M.; Rodríguez, H.; Curiel, J.A.; de las Rivas, B.; de Felipe, F.L.; Muñoz, R. Degradation of Phenolic Compounds Found in Olive Products by Lactobacillus plantarum Strains. In Olives and Olive Oil in Health and Disease Prevention; Elsevier: Amsterdam, The Netherlands, 2010; pp. 387–396. [Google Scholar]
  85. Pino, A.; Vaccalluzzo, A.; Solieri, L.; Romeo, F.V.; Todaro, A.; Caggia, C.; Arroyo-López, F.N.; Bautista-Gallego, J.; Randazzo, C.L. Effect of Sequential Inoculum of Beta-Glucosidase Positive and Probiotic Strains on Brine Fermentation to Obtain Low Salt Sicilian Table Olives. Front. Microbiol. 2019, 10, 174. [Google Scholar] [CrossRef]
  86. Servili, M.; Settanni, L.; Veneziani, G.; Esposto, S.; Massitti, O.; Taticchi, A.; Urbani, S.; Montedoro, G.F.; Corsetti, A. The Use of Lactobacillus pentosus 1MO To Shorten the Debittering Process Time of Black Table Olives (Cv. Itrana and Leccino): A Pilot-Scale Application. J. Agric. Food Chem. 2006, 54, 3869–3875. [Google Scholar] [CrossRef]
  87. De Leonardis, A.; Testa, B.; Macciola, V.; Lombardi, S.J.; Iorizzo, M. Exploring Enzyme and Microbial Technology for the Preparation of Green Table Olives. Eur. Food Res. Technol. 2016, 242, 363–370. [Google Scholar] [CrossRef]
  88. Grimaldi, A.; Bartowsky, E.; Jiranek, V. Screening of Lactobacillus Spp. and Pediococcus Spp. for Glycosidase Activities That Are Important in Oenology. J. Appl. Microbiol. 2005, 99, 1061–1069. [Google Scholar] [CrossRef]
  89. Grimaldi, A.; McLean, H.; Jiranek, V. Identification and Partial Characterization of Glycosidic Activities of Commercial Strains of the Lactic Acid Bacterium, Oenococcus oeni. Am. J. Enol. Vitic. 2000, 51, 362–369. [Google Scholar] [CrossRef]
  90. Zhang, J.; Zhao, N.; Xu, J.; Qi, Y.; Wei, X.; Fan, M. Homology Analysis of 35 β-Glucosidases in Oenococcus Oeni and Biochemical Characterization of a Novel β-Glucosidase BGL0224. Food Chem. 2021, 334, 127593. [Google Scholar] [CrossRef]
  91. Maturano, C.; Saguir, F.M. Influence of Glycosides on Behavior of Oenococcus Oeni in Wine Conditions: Growth, Substrates and Aroma Compounds. World J. Microbiol. Biotechnol. 2017, 33, 151. [Google Scholar] [CrossRef]
  92. Michlmayr, H.; Schümann, C.; Wurbs, P.; Barreira Braz da Silva, N.M.; Rogl, V.; Kulbe, K.D.; del Hierro, A.M. A β-Glucosidase from Oenococcus Oeni ATCC BAA-1163 with Potential for Aroma Release in Wine: Cloning and Expression in E. coli. World J. Microbiol. Biotechnol. 2010, 26, 1281–1289. [Google Scholar] [CrossRef]
  93. D’Incecco, N.; Bartowsky, E.; Kassara, S.; Lante, A.; Spettoli, P.; Henschke, P. Release of Glycosidically Bound Flavour Compounds of Chardonnay by Oenococcus Oeni during Malolactic Fermentation. Food Microbiol. 2004, 21, 257–265. [Google Scholar] [CrossRef]
  94. Iorizzo, M.; Testa, B.; Lombardi, S.J.; García-Ruiz, A.; Muñoz-González, C.; Bartolomé, B.; Moreno-Arribas, M.V. Selection and Technological Potential of Lactobacillus plantarum Bacteria Suitable for Wine Malolactic Fermentation and Grape Aroma Release. LWT 2016, 73, 557–566. [Google Scholar] [CrossRef]
  95. Liu, L.; Zhang, C.; Zhang, H.; Qu, G.; Li, C.; Liu, L. Biotransformation of Polyphenols in Apple Pomace Fermented by β-Glucosidase-Producing Lactobacillus rhamnosus L08. Foods 2021, 10, 1343. [Google Scholar] [CrossRef]
  96. Modrackova, N.; Vlkova, E.; Tejnecky, V.; Schwab, C.; Neuzil-Bunesova, V. Bifidobacterium β-Glucosidase Activity and Fermentation of Dietary Plant Glucosides Is Species and Strain Specific. Microorganisms 2020, 8, 839. [Google Scholar] [CrossRef]
  97. Di Cagno, R.; Filannino, P.; Gobbetti, M. Lactic Acid Fermentation Drives the Optimal Volatile Flavor-Aroma Profile of Pomegranate Juice. Int. J. Food Microbiol. 2017, 248, 56–62. [Google Scholar] [CrossRef]
  98. Martorana, A.; Alfonzo, A.; Gaglio, R.; Settanni, L.; Corona, O.; La Croce, F.; Vagnoli, P.; Caruso, T.; Moschetti, G.; Francesca, N. Evaluation of Different Conditions to Enhance the Performances of Lactobacillus Pentosus OM13 during Industrial Production of Spanish-Style Table Olives. Food Microbiol. 2017, 61, 150–158. [Google Scholar] [CrossRef]
  99. Lei, V.; Amoa-Awua, W.K.A.; Brimer, L. Degradation of Cyanogenic Glycosides by Lactobacillus plantarum Strains from Spontaneous Cassava Fermentation and Other Microorganisms. Int. J. Food Microbiol. 1999, 53, 169–184. [Google Scholar] [CrossRef]
  100. Menon, R.; Munjal, N.; Sturino, J.M. Characterization of Amygdalin-Degrading Lactobacillus Species. J. Appl. Microbiol. 2015, 118, 443–453. [Google Scholar] [CrossRef]
  101. Gunawan, S.; Widjaja, T.; Zullaikah, S.; Ernawati, L.; Istianah, N.; Aparamarta, H.W.; Prasetyoko, D. Effect of Fermenting Cassava with Lactobacillus plantarum, Saccharomyces Cereviseae, and Rhizopus Oryzae on the Chemical Composition of Their Flour. Int. Food Res. J. 2015, 22, 1280–1287. [Google Scholar]
  102. Bustamante-Rangel, M.; Delgado-Zamarreño, M.M.; Pérez-Martín, L.; Rodríguez-Gonzalo, E.; Domínguez-Álvarez, J. Analysis of Isoflavones in Foods. Compr. Rev. Food Sci. Food Saf. 2018, 17, 391–411. [Google Scholar] [CrossRef] [PubMed]
  103. Atlante, A.; Bobba, A.; Paventi, G.; Pizzuto, R.; Passarella, S. Genistein and Daidzein Prevent Low Potassium-Dependent Apoptosis of Cerebellar Granule Cells. Biochem. Pharmacol. 2010, 79, 758–767. [Google Scholar] [CrossRef]
  104. Sharma, D.; Singh, V.; Kumar, A.; Singh, T.G. Genistein: A Promising Ally in Combating Neurodegenerative Disorders. Eur. J. Pharmacol. 2025, 991, 177273. [Google Scholar] [CrossRef]
  105. Zaheer, K.; Humayoun Akhtar, M. An Updated Review of Dietary Isoflavones: Nutrition, Processing, Bioavailability and Impacts on Human Health. Crit. Rev. Food Sci. Nutr. 2017, 57, 1280–1293. [Google Scholar] [CrossRef]
  106. Jayachandran, M.; Xu, B. An Insight into the Health Benefits of Fermented Soy Products. Food Chem. 2019, 271, 362–371. [Google Scholar] [CrossRef]
  107. Hu, C.; Wong, W.T.; Wu, R.; Lai, W.F. Biochemistry and Use of Soybean Isoflavones in Functional Food Development. Crit. Rev. Food Sci. Nutr. 2020, 60, 2098–2112. [Google Scholar] [CrossRef]
  108. Jung, Y.S.; Rha, C.-S.; Baik, M.-Y.; Baek, N.-I.; Kim, D.-O. A Brief History and Spectroscopic Analysis of Soy Isoflavones. Food Sci. Biotechnol. 2020, 29, 1605–1617. [Google Scholar] [CrossRef]
  109. Izumi, T.; Osawa, S.; Obata, A.; Tobe, K.; Saito, M.; Kataoka, S.; Kikuchi, M.; Piskula, M.K.; Kubota, Y. Soy Isoflavone Aglycones Are Absorbed Faster and in Higher Amounts than Their Glucosides in Humans. J. Nutr. 2000, 130, 1695–1699. [Google Scholar] [CrossRef]
  110. Liu, H.; Wang, Y.; Zhu, D.; Xu, J.; Xu, X.; Liu, J. Bioaccessibility and Application of Soybean Isoflavones: A Review. Food Rev. Int. 2022, 39, 5948–5967. [Google Scholar] [CrossRef]
  111. Setchell, K.D.; Brown, N.M.; Zimmer-Nechemias, L.; Brashear, W.T.; Wolfe, B.E.; Kirschner, A.S.; Heubi, J.E. Evidence for Lack of Absorption of Soy Isoflavone Glycosides in Humans, Supporting the Crucial Role of Intestinal Metabolism for Bioavailability. Am. J. Clin. Nutr. 2002, 76, 447–453. [Google Scholar] [CrossRef] [PubMed]
  112. Chien, H.-L.; Huang, H.-Y.; Chou, C.-C. Transformation of Isoflavone Phytoestrogens during the Fermentation of Soymilk with Lactic Acid Bacteria and Bifidobacteria. Food Microbiol. 2006, 23, 772–778. [Google Scholar] [CrossRef] [PubMed]
  113. Chun, J.; Kim, G.M.; Lee, K.W.; Choi, I.D.; Kwon, G.; Park, J.; Jeong, S.; Kim, J.; Kim, J.H. Conversion of Isoflavone Glucosides to Aglycones in Soymilk by Fermentation with Lactic Acid Bacteria. J. Food Sci. 2007, 72, M39–M44. [Google Scholar] [CrossRef]
  114. Pyo, Y.-H.; Lee, T.-C.; Lee, Y.-C. Enrichment of Bioactive Isoflavones in Soymilk Fermented with β-Glucosidase-Producing Lactic Acid Bacteria. Food Res. Int. 2005, 38, 551–559. [Google Scholar] [CrossRef]
  115. Lim, Y.J.; Lim, B.; Kim, H.Y.; Kwon, S.-J.; Eom, S.H. Deglycosylation Patterns of Isoflavones in Soybean Extracts Inoculated with Two Enzymatically Different Strains of Lactobacillus Species. Enzym. Microb. Technol. 2020, 132, 109394. [Google Scholar] [CrossRef] [PubMed]
  116. Tang, A.L.; Shah, N.P.; Wilcox, G.; Walker, K.Z.; Stojanovska, L. Fermentation of Calcium-Fortified Soymilk with Lactobacillus: Effects on Calcium Solubility, Isoflavone Conversion, and Production of Organic Acids. J. Food Sci. 2007, 72, M431–M436. [Google Scholar] [CrossRef]
  117. Du, L.; Ro, K.-S.; Zhang, Y.; Tang, Y.-J.; Li, W.; Xie, J.; Wei, D. Effects of Lactiplantibacillus plantarum X7021 on Physicochemical Properties, Purines, Isoflavones and Volatile Compounds of Fermented Soymilk. Process Biochem. 2022, 113, 150–157. [Google Scholar] [CrossRef]
  118. Hidayati, D.; Soetjipto, S.; Catur Adi, A. Characteristic and Isoflavone Level of Soymilk Fermented by Single and Mixed Culture of Lactobacillus plantarum and Yoghurt Starter. J. Food Nutr. Res. 2021, 9, 55–60. [Google Scholar] [CrossRef]
  119. Izaguirre, J.K.; Barañano, L.; Castañón, S.; Alkorta, I.; Quirós, L.M.; Garbisu, C. Optimization of the Bioactivation of Isoflavones in Soymilk by Lactic Acid Bacteria. Processes 2021, 9, 963. [Google Scholar] [CrossRef]
  120. Bock, H.-J.; Lee, H.-W.; Lee, N.-K.; Paik, H.-D. Probiotic Lactiplantibacillus plantarum KU210152 and Its Fermented Soy Milk Attenuates Oxidative Stress in Neuroblastoma Cells. Food Res. Int. 2024, 177, 113868. [Google Scholar] [CrossRef]
  121. Choi, G.-H.; Bock, H.-J.; Lee, N.-K.; Paik, H.-D. Soy Yogurt Using Lactobacillus plantarum 200655 and Fructooligosaccharides: Neuroprotective Effects against Oxidative Stress. J. Food Sci. Technol. 2022, 59, 4870–4879. [Google Scholar] [CrossRef] [PubMed]
  122. Wang, A.; Hou, K.; Mu, G.; Ma, C.; Tuo, Y. Antioxidative Effect of Soybean Milk Fermented by Lactobacillus plantarum Y16 on 2, 2-Azobis (2-Methylpropionamidine) Dihydrochloride (ABAP)-Damaged HepG2 Cells. Food Biosci. 2021, 44, 101120. [Google Scholar] [CrossRef]
  123. Peng, H.T.; Yang, C.Y.; Fang, T.J. Enhanced β-Glucosidase Activity of Lactobacillus plantarum by a Strategic Ultrasound Treatment for Biotransformation of Isoflavones in Okara. Food Sci. Technol. Res. 2018, 24, 777–784. [Google Scholar] [CrossRef]
  124. Wang, R.; Thakur, K.; Feng, J.-Y.; Zhu, Y.-Y.; Zhang, F.; Russo, P.; Spano, G.; Zhang, J.-G.; Wei, Z.-J. Functionalization of Soy Residue (Okara) by Enzymatic Hydrolysis and LAB Fermentation for B2 Bio-Enrichment and Improved in Vitro Digestion. Food Chem. 2022, 387, 132947. [Google Scholar] [CrossRef]
  125. Parmar, A.; Sturm, B.; Hensel, O. Crops That Feed the World: Production and Improvement of Cassava for Food, Feed, and Industrial Uses. Food Secur. 2017, 9, 907–927. [Google Scholar] [CrossRef]
  126. Malik, A.I.; Kongsil, P.; Nguyễn, V.A.; Ou, W.; Sholihin; Srean, P.; Sheela, M.; Becerra López-Lavalle, L.A.; Utsumi, Y.; Lu, C.; et al. Cassava Breeding and Agronomy in Asia: 50 Years of History and Future Directions. Breed. Sci. 2020, 70, 145–166. [Google Scholar] [CrossRef]
  127. Halake, N.H.; Chinthapalli, B. Fermentation of Traditional African Cassava Based Foods: Microorganisms Role in Nutritional and Safety Value. J. Exp. Agric. Int. 2020, 42, 56–65. [Google Scholar] [CrossRef]
  128. Lacerda, I.; Miranda, R.; Borelli, B.; Nunes, A.; Nardi, R.; Lachance, M.; Rosa, C. Lactic Acid Bacteria and Yeasts Associated with Spontaneous Fermentations during the Production of Sour Cassava Starch in Brazil. Int. J. Food Microbiol. 2005, 105, 213–219. [Google Scholar] [CrossRef]
  129. Howeler, R.; Lutaladio, N.; Thomas, G. Save and Grow: Cassava: A Guide to Sustainable Production Intensification; Food and Agriculture Organization of the United Nations: Rome, Italy, 2013. [Google Scholar]
  130. Latif, S.; Müller, J. Potential of Cassava Leaves in Human Nutrition: A Review. Trends Food Sci. Technol. 2015, 44, 147–158. [Google Scholar] [CrossRef]
  131. Adebayo, W.G. Cassava Production in Africa: A Panel Analysis of the Drivers and Trends. Heliyon 2023, 9, e19939. [Google Scholar] [CrossRef]
  132. Kashala-Abotnes, E.; Okitundu, D.; Mumba, D.; Boivin, M.J.; Tylleskär, T.; Tshala-Katumbay, D. Konzo: A Distinct Neurological Disease Associated with Food (Cassava) Cyanogenic Poisoning. Brain Res. Bull. 2019, 145, 87–91. [Google Scholar] [CrossRef]
  133. Adamolekun, B. Neurological Disorders Associated with Cassava Diet: A Review of Putative Etiological Mechanisms. Metab. Brain Dis. 2011, 26, 79–85. [Google Scholar] [CrossRef]
  134. Fukushima, A.R.; Nicoletti, M.A.; Rodrigues, A.J.; Pressutti, C.; Almeida, J.; Brandão, T.; Kinue Ito, R.; Bafille Leoni, L.A.; Souza Spinosa, H. De Cassava Flour: Quantification of Cyanide Content. Food Nutr. Sci. 2016, 07, 592–599. [Google Scholar] [CrossRef]
  135. Cressey, P.; Reeve, J. Metabolism of Cyanogenic Glycosides: A Review. Food Chem. Toxicol. 2019, 125, 225–232. [Google Scholar] [CrossRef] [PubMed]
  136. Renchinkhand, G.; Park, Y.W.; Cho, S.-H.; Song, G.-Y.; Bae, H.C.; Choi, S.-J.; Nam, M.S. Identification of β-Glucosidase Activity of Lactobacillus plantarum CRNB22 in Kimchi and Its Potential to Convert Ginsenoside Rb1 from Panax ginseng. J. Food Biochem. 2015, 39, 155–163. [Google Scholar] [CrossRef]
  137. National Research Council. Acute Exposure Guideline Levels for Selected Airborne Chemicals; National Academies Press: Washington, DC, USA, 2002; ISBN 978-0-309-08511-3. [Google Scholar]
  138. Oloya, B.; Adaku, C.; Andama, M. The Cyanogenic Potential of Certain Cassava Varieties in Uganda and Their Fermentation-Based Detoxification. In Cassava—Recent Updates on Food, Feed, and Industry; IntechOpen: London, UK, 2024. [Google Scholar]
  139. Brimer, L. Cassava Production and Processing and Impact on Biological Compounds; Academic Press: Cambridge, MA, USA, 2015; ISBN 9780124047099. [Google Scholar]
  140. Penido, F.C.L.; Piló, F.B.; Sandes, S.H.d.C.; Nunes, Á.C.; Colen, G.; Oliveira, E.D.S.; Rosa, C.A.; Lacerda, I.C.A. Selection of Starter Cultures for the Production of Sour Cassava Starch in a Pilot-Scale Fermentation Process. Braz. J. Microbiol. 2018, 49, 823–831. [Google Scholar] [CrossRef]
  141. Bouatenin, K.M.J.-P.; Theodore, D.N.; Alfred, K.K.; Hermann, C.W.; Marcellin, D.K. Excretion of β-Glucosidase and Pectinase by Microorganisms Isolated from Cassava Traditional Ferments Used for Attieke Production in Côte d’Ivoire. Biocatal. Agric. Biotechnol. 2019, 20, 101217. [Google Scholar] [CrossRef]
  142. Panghal, A.; Munezero, C.; Sharma, P.; Chhikara, N. Cassava Toxicity, Detoxification and Its Food Applications: A Review. Toxin Rev. 2021, 40, 1–16. [Google Scholar] [CrossRef]
  143. Ben Omar, N.; Ampe, F.; Raimbault, M.; Guyot, J.-P.; Tailliez, P. Molecular Diversity of Lactic Acid Bacteria from Cassava Sour Starch (Colombia). Syst. Appl. Microbiol. 2000, 23, 285–291. [Google Scholar] [CrossRef] [PubMed]
  144. Bamigbade, G.B.; Sanusi, J.F.O.; Oyelami, O.I.; Daniel, O.M.; Alimi, B.O.; Ampofo, K.A.; Liu, S.-Q.; Shah, N.P.; Ayyash, M. Identification and Characterization of Lactic Acid Bacteria Isolated from Effluents Generated During Cassava Fermentation as Potential Candidates for Probiotics. Food Biotechnol. 2023, 37, 413–433. [Google Scholar] [CrossRef]
  145. Oyedeji, O.; Ogunbanwo, S.T.; Onilude, A.A. Predominant Lactic Acid Bacteria Involved in the Traditional Fermentation of Fufu and Ogi, Two Nigerian Fermented Food Products. Food Nutr. Sci. 2013, 04, 40–46. [Google Scholar] [CrossRef]
  146. Putri, W.D.R.; Haryadi; Marseno, D.W.; Cahyanto, M.N. Role of Lactic Acid Bacteria on Structural and Physicochemical Properties of Sour Cassava Starch. APCBEE Procedia 2012, 2, 104–109. [Google Scholar] [CrossRef]
  147. Crispim, S.M.; Nascimento, A.M.A.; Costa, P.S.; Moreira, J.L.S.; Nunes, A.C.; Nicoli, J.R.; Lima, F.L.; Mota, V.T.; Nardi, R.M.D. Molecular Identification of Lactobacillus Spp. Associated with Puba, a Brazilian Fermented Cassava Food. Braz. J. Microbiol. 2013, 44, 15–21. [Google Scholar] [CrossRef]
  148. Wilfrid Padonou, S.; Nielsen, D.S.; Hounhouigan, J.D.; Thorsen, L.; Nago, M.C.; Jakobsen, M. The Microbiota of Lafun, an African Traditional Cassava Food Product. Int. J. Food Microbiol. 2009, 133, 22–30. [Google Scholar] [CrossRef]
  149. Figueroa, C.; Davila, A.M.; Pourquié, J. Lactic Acid Bacteria of the Sour Cassava Starch Fermentation. Lett. Appl. Microbiol. 1995, 21, 126–130. [Google Scholar] [CrossRef]
  150. Kostinek, M.; Specht, I.; Edward, V.A.; Pinto, C.; Egounlety, M.; Sossa, C.; Mbugua, S.; Dortu, C.; Thonart, P.; Taljaard, L.; et al. Characterisation and Biochemical Properties of Predominant Lactic Acid Bacteria from Fermenting Cassava for Selection as Starter Cultures. Int. J. Food Microbiol. 2007, 114, 342–351. [Google Scholar] [CrossRef] [PubMed]
  151. Wakil, S.M.; Benjamin, I.B. Starter Developed Pupuru, a Traditional Africa Fermented Food from Cassava (Manihot Esculenta). Int. Food Res. J. 2015, 22, 2565–2570. [Google Scholar]
  152. Kostinek, M.; Specht, I.; Edward, V.A.; Schillinger, U.; Hertel, C.; Holzapfel, W.H.; Franz, C.M.A.P. Diversity and Technological Properties of Predominant Lactic Acid Bacteria from Fermented Cassava Used for the Preparation of Gari, a Traditional African Food. Syst. Appl. Microbiol. 2005, 28, 527–540. [Google Scholar] [CrossRef] [PubMed]
  153. Tefera, T.; Ameha, K.; Biruhtesfa, A. Cassava Based Foods: Microbial Fermentation by Single Starter Culture towards Cyanide Reduction, Protein Enhancement and Palatability. Int. Food Res. J. 2014, 21, 1751–1756. [Google Scholar]
  154. Kimaryo, V.M.; Massawe, G.A.; Olasupo, N.A.; Holzapfel, W.H. The Use of a Starter Culture in the Fermentation of Cassava for the Production of “Kivunde”, a Traditional Tanzanian Food Product. Int. J. Food Microbiol. 2000, 56, 179–190. [Google Scholar] [CrossRef]
  155. Damayanti, E.; Kurniadi, M.; Helmi, R.L.; Frediansyah, A. Single Starter Lactobacillus plantarum for Modified Cassava Flour (Mocaf) Fermentation. In Proceedings of the IOP Conference Series: Earth and Environmental Science, Changsha, China, 18–20 September 2020; Volume 462. [Google Scholar]
  156. Charoenprasert, S.; Mitchell, A. Factors Influencing Phenolic Compounds in Table Olives (Olea Europaea). J. Agric. Food Chem. 2012, 60, 7081–7095. [Google Scholar] [CrossRef] [PubMed]
  157. Guggenheim, K.G.; Crawford, L.M.; Paradisi, F.; Wang, S.C.; Siegel, J.B. β-Glucosidase Discovery and Design for the Degradation of Oleuropein. ACS Omega 2018, 3, 15754–15762. [Google Scholar] [CrossRef]
  158. Rokni, Y.; Abouloifa, H.; Bellaouchi, R.; Gaamouche, S.; Mchiouer, K.; Hasnaoui, I.; Lamzira, Z.; Ghabbour, N.; Asehraou, A. Technological Process of Fermented Olive. Arab. J. Chem. Environ. Res. 2017, 07, 63–91. [Google Scholar]
  159. Habibi, M.; Golmakani, M.-T.; Farahnaky, A.; Mesbahi, G.; Majzoobi, M. NaOH-Free Debittering of Table Olives Using Power Ultrasound. Food Chem. 2016, 192, 775–781. [Google Scholar] [CrossRef]
  160. Corsetti, A.; Perpetuini, G.; Schirone, M.; Tofalo, R.; Suzzi, G. Application of Starter Cultures to Table Olive Fermentation: An Overview on the Experimental Studies. Front. Microbiol. 2012, 3, 248. [Google Scholar] [CrossRef] [PubMed]
  161. Ciafardini, G.; Marsilio, V.; Lanza, B.; Pozzi, N. Hydrolysis of Oleuropein by Lactobacillus plantarum Strains Associated with Olive Fermentation. Appl. Environ. Microbiol. 1994, 60, 4142–4147. [Google Scholar] [CrossRef]
  162. Rokni, Y.; Abouloifa, H.; Bellaouchi, R.; Hasnaoui, I.; Gaamouche, S.; Lamzira, Z.; Salah, R.B.E.N.; Saalaoui, E.; Ghabbour, N.; Asehraou, A. Characterization of β-Glucosidase of Lactobacillus plantarum FSO1 and Candida Pelliculosa L18 Isolated from Traditional Fermented Green Olive. J. Genet. Eng. Biotechnol. 2021, 19, 117. [Google Scholar] [CrossRef]
  163. Ghabbour, N.; Rokni, Y.; Abouloifa, H.; Bellaouchi, R.; Chihib, N.-E.; Ben Salah, R.; Lamzira, Z.; Saalaoui, E.; Asehraou, A. In Vitro Biodegradation of Oleuropein by Lactobacillus plantarum FSO175 in Stress Conditions (pH, NaCl and Glucose). J. Microbiol. Biotechnol. Food Sci. 2020, 9, 769–773. [Google Scholar] [CrossRef]
  164. Ghabbour, N.; Rokni, Y.; Lamzira, Z.; Thonart, P.; Chihib, N.E.; Peres, C.; Asehraou, A. Controlled Fermentation of Moroccan Picholine Green Olives by Oleuropein-Degrading Lactobacilli Strains. Grasas Aceites 2016, 67, e138. [Google Scholar] [CrossRef]
  165. Vaccalluzzo, A.; Pino, A.; De Angelis, M.; Bautista-Gallego, J.; Romeo, F.V.; Foti, P.; Caggia, C.; Randazzo, C.L. Effects of Different Stress Parameters on Growth and on Oleuropein-Degrading Abilities of Lactiplantibacillus plantarum Strains Selected as Tailored Starter Cultures for Naturally Table Olives. Microorganisms 2020, 8, 1607. [Google Scholar] [CrossRef]
  166. Zago, M.; Lanza, B.; Rossetti, L.; Muzzalupo, I.; Carminati, D.; Giraffa, G. Selection of Lactobacillus plantarum Strains to Use as Starters in Fermented Table Olives: Oleuropeinase Activity and Phage Sensitivity. Food Microbiol. 2013, 34, 81–87. [Google Scholar] [CrossRef]
  167. Vaccalluzzo, A.; Solieri, L.; Tagliazucchi, D.; Cattivelli, A.; Martini, S.; Pino, A.; Caggia, C.; Randazzo, C.L. Metabolomic and Transcriptional Profiling of Oleuropein Bioconversion into Hydroxytyrosol during Table Olive Fermentation by Lactiplantibacillus plantarum. Appl. Environ. Microbiol. 2022, 88, e0201921. [Google Scholar] [CrossRef]
  168. Romeo, F.V.; Granuzzo, G.; Foti, P.; Ballistreri, G.; Caggia, C.; Rapisarda, P. Microbial Application to Improve Olive Mill Wastewater Phenolic Extracts. Molecules 2021, 26, 1944. [Google Scholar] [CrossRef]
  169. Sciurba, L.; Indelicato, S.; Gaglio, R.; Barbera, M.; Marra, F.P.; Bongiorno, D.; Davino, S.; Piazzese, D.; Settanni, L.; Avellone, G. Analysis of Olive Oil Mill Wastewater from Conventionally Farmed Olives: Chemical and Microbiological Safety and Polyphenolic Profile for Possible Use in Food Product Functionalization. Foods 2025, 14, 449. [Google Scholar] [CrossRef]
  170. Cappello, M.S.; Zapparoli, G.; Logrieco, A.; Bartowsky, E.J. Linking Wine Lactic Acid Bacteria Diversity with Wine Aroma and Flavour. Int. J. Food Microbiol. 2017, 243, 16–27. [Google Scholar] [CrossRef]
  171. Virdis, C.; Sumby, K.; Bartowsky, E.; Jiranek, V. Lactic Acid Bacteria in Wine: Technological Advances and Evaluation of Their Functional Role. Front. Microbiol. 2021, 11, 612118. [Google Scholar] [CrossRef]
  172. Boido, E.; Lloret, A.; Medina, K.; Carrau, F.; Dellacassa, E. Effect of β-Glycosidase Activity of Oenococcus oeni on the Glycosylated Flavor Precursors of Tannat Wine during Malolactic Fermentation. J. Agric. Food Chem. 2002, 50, 2344–2349. [Google Scholar] [CrossRef]
  173. Swiegers, J.H.; Bartowsky, E.J.; Henschke, P.A.; Pretorius, I.S. Yeast and Bacterial Modulation of Wine Aroma and Flavour. Aust. J. Grape Wine Res. 2005, 11, 139–173. [Google Scholar] [CrossRef]
  174. Bartowsky, E.J.; Costello, P.J.; Chambers, P.J. Emerging Trends in the Application of Malolactic Fermentation. Aust. J. Grape Wine Res. 2015, 21, 663–669. [Google Scholar] [CrossRef]
  175. du Toit, M.; Engelbrecht, L.; Lerm, E.; Krieger-Weber, S. Lactobacillus: The Next Generation of Malolactic Fermentation Starter Cultures—An Overview. Food Bioprocess Techol. 2011, 4, 876–906. [Google Scholar] [CrossRef]
  176. Krieger-Weber, S.; Heras, J.M.; Suarez, C. Lactobacillus plantarum, a New Biological Tool to Control Malolactic Fermentation: A Review and an Outlook. Beverages 2020, 6, 23. [Google Scholar] [CrossRef]
  177. Berbegal, C.; Peña, N.; Russo, P.; Grieco, F.; Pardo, I.; Ferrer, S.; Spano, G.; Capozzi, V. Technological Properties of Lactobacillus plantarum Strains Isolated from Grape Must Fermentation. Food Microbiol. 2016, 57, 187–194. [Google Scholar] [CrossRef] [PubMed]
  178. Succi, M.; Pannella, G.; Tremonte, P.; Tipaldi, L.; Coppola, R.; Iorizzo, M.; Lombardi, S.J.; Sorrentino, E. Sub-Optimal pH Preadaptation Improves the Survival of Lactobacillus plantarum Strains and the Malic Acid Consumption in Wine-like Medium. Front. Microbiol. 2017, 8, 470. [Google Scholar] [CrossRef]
  179. Tufariello, M.; Capozzi, V.; Spano, G.; Cantele, G.; Venerito, P.; Mita, G.; Grieco, F. Effect of Co-Inoculation of Candida zemplinina, Saccharomyces cerevisiae and Lactobacillus plantarum for the Industrial Production of Negroamaro Wine in Apulia (Southern Italy). Microorganisms 2020, 8, 726. [Google Scholar] [CrossRef]
  180. Pannella, G.; Lombardi, S.J.; Coppola, F.; Vergalito, F.; Iorizzo, M.; Succi, M.; Tremonte, P.; Iannini, C.; Sorrentino, E.; Coppola, R. Effect of Biofilm Formation by Lactobacillus plantarum on the Malolactic Fermentation in Model Wine. Foods 2020, 9, 797. [Google Scholar] [CrossRef]
  181. Bravo-Ferrada, B.M.; Hollmann, A.; Delfederico, L.; Valdés La Hens, D.; Caballero, A.; Semorile, L. Patagonian Red Wines: Selection of Lactobacillus plantarum Isolates as Potential Starter Cultures for Malolactic Fermentation. World J. Microbiol. Biotechnol. 2013, 29, 1537–1549. [Google Scholar] [CrossRef]
  182. Balmaseda, A.; Rozès, N.; Bordons, A.; Reguant, C. Characterization of Malolactic Fermentation by Lactiplantibacillus plantarum in Red Grape Must. LWT 2024, 199, 116070. [Google Scholar] [CrossRef]
  183. Lombardi, S.J.; Pannella, G.; Iorizzo, M.; Testa, B.; Succi, M.; Tremonte, P.; Sorrentino, E.; Di Renzo, M.; Strollo, D.; Coppola, R. Inoculum Strategies and Performances of Malolactic Starter Lactobacillus plantarum M10: Impact on Chemical and Sensorial Characteristics of Fiano Wine. Microorganisms 2020, 8, 516. [Google Scholar] [CrossRef]
  184. Devi, A.; Anu-Appaiah, K.A.; Lin, T.F. Timing of Inoculation of Oenococcus Oeni and Lactobacillus plantarum in Mixed Malo-Lactic Culture along with Compatible Native Yeast Influences the Polyphenolic, Volatile and Sensory Profile of the Shiraz Wines. LWT 2022, 158, 113130. [Google Scholar] [CrossRef]
  185. Brizuela, N.; Tymczyszyn, E.E.; Semorile, L.C.; Valdes La Hens, D.; Delfederico, L.; Hollmann, A.; Bravo-Ferrada, B. Lactobacillus plantarum as a Malolactic Starter Culture in Winemaking: A New (Old) Player? Electron. J. Biotechnol. 2019, 38, 10–18. [Google Scholar] [CrossRef]
  186. Brizuela, N.S.; Franco-Luesma, E.; Bravo-Ferrada, B.M.; Pérez-Jiménez, M.; Semorile, L.; Tymczyszyn, E.E.; Pozo-Bayon, M.A. Influence of Patagonian Lactiplantibacillus plantarum and Oenococcus oeni Strains on Sensory Perception of Pinot Noir Wine after Malolactic Fermentation. Aust. J. Grape Wine Res. 2021, 27, 118–127. [Google Scholar] [CrossRef]
  187. Sestelo, A.B.F.; Poza, M.; Villa, T.G. β-Glucosidase Activity in a Lactobacillus plantarum Wine Strain. World J. Microbiol. Biotechnol. 2004, 20, 633–637. [Google Scholar] [CrossRef]
  188. Brizuela, N.S.; Arnez-Arancibia, M.; Semorile, L.; Pozo-Bayón, M.Á.; Bravo-Ferrada, B.M.; Elizabeth Tymczyszyn, E. β-Glucosidase Activity of Lactiplantibacillus plantarum UNQLp 11 in Different Malolactic Fermentations Conditions: Effect of pH and Ethanol Content. Fermentation 2021, 7, 22. [Google Scholar] [CrossRef]
  189. Gouripur, G.; Kaliwal, B. Screening and Optimization of β-Glucosidase Producing Newly Isolated Lactobacillus plantarum Strain LSP-24 from Colostrum Milk. Biocatal. Agric. Biotechnol. 2017, 11, 89–96. [Google Scholar] [CrossRef]
  190. Barbagallo, R.N.; Spagna, G.; Palmeri, R.; Restuccia, C.; Giudici, P. Selection, Characterization and Comparison of β-Glucosidase from Mould and Yeasts Employable for Enological Applications. Enzym. Microb. Technol. 2004, 35, 58–66. [Google Scholar] [CrossRef]
  191. Olguín, N.; Alegret, J.O.; Bordons, A.; Reguant, C. β-Glucosidase Activity and Bgl Gene Expression of Oenococcus Oeni Strains in Model Media and Cabernet Sauvignon Wine. Am. J. Enol. Vitic. 2011, 62, 99–105. [Google Scholar] [CrossRef]
  192. Fia, G.; Millarini, V.; Granchi, L.; Bucalossi, G.; Guerrini, S.; Zanoni, B.; Rosi, I. Beta-Glucosidase and Esterase Activity from Oenococcus Oeni: Screening and Evaluation during Malolactic Fermentation in Harsh Conditions. LWT 2018, 89, 262–268. [Google Scholar] [CrossRef]
  193. Lorn, D.; Nguyen, T.-K.-C.; Ho, P.-H.; Tan, R.; Licandro, H.; Waché, Y. Screening of Lactic Acid Bacteria for Their Potential Use as Aromatic Starters in Fermented Vegetables. Int. J. Food Microbiol. 2021, 350, 109242. [Google Scholar] [CrossRef]
  194. Landete, J.M.; Curiel, J.A.; Rodríguez, H.; de las Rivas, B.; Muñoz, R. Aryl Glycosidases from Lactobacillus plantarum Increase Antioxidant Activity of Phenolic Compounds. J. Funct. Foods 2014, 7, 322–329. [Google Scholar] [CrossRef]
  195. Wang, S.-Y.; Zhu, H.-Z.; Lan, Y.-B.; Liu, R.-J.; Liu, Y.-R.; Zhang, B.-L.; Zhu, B.-Q. Modifications of Phenolic Compounds, Biogenic Amines, and Volatile Compounds in Cabernet Gernishct Wine through Malolactic Fermentation by Lactobacillus plantarum and Oenococcus oeni. Fermentation 2020, 6, 15. [Google Scholar] [CrossRef]
  196. Van Oevelen, D.; Spaepen, M.; Timmermans, P.; Verachtert, H. Microbiological Aspects of Spontaneous Wort Fermentation in the Production of Lambic and Gueuze. J. Inst. Brew. 1977, 83, 356–360. [Google Scholar] [CrossRef]
  197. Dysvik, A.; La Rosa, S.L.; De Rouck, G.; Rukke, E.-O.; Westereng, B.; Wicklund, T. Microbial Dynamics in Traditional and Modern Sour Beer Production. Appl. Environ. Microbiol. 2020, 86, e00566-20. [Google Scholar] [CrossRef]
  198. Testa, B.; Coppola, F.; Letizia, F.; Albanese, G.; Karaulli, J.; Ruci, M.; Pistillo, M.; Germinara, G.S.; Messia, M.C.; Succi, M.; et al. Versatility of Saccharomyces Cerevisiae 41CM in the Brewery Sector: Use as a Starter for “Ale” and “Lager” Craft Beer Production. Processes 2022, 10, 2495. [Google Scholar] [CrossRef]
  199. Karaulli, J.; Xhaferaj, N.; Coppola, F.; Testa, B.; Letizia, F.; Kyçyk, O.; Kongoli, R.; Ruci, M.; Lamçe, F.; Sulaj, K.; et al. Bioprospecting of Metschnikowia pulcherrima Strains, Isolated from a Vineyard Ecosystem, as Novel Starter Cultures for Craft Beer Production. Fermentation 2024, 10, 513. [Google Scholar] [CrossRef]
  200. Iorizzo, M.; Letizia, F.; Albanese, G.; Coppola, F.; Gambuti, A.; Testa, B.; Aversano, R.; Forino, M.; Coppola, R. Potential for Lager Beer Production from Saccharomyces Cerevisiae Strains Isolated from the Vineyard Environment. Processes 2021, 9, 1628. [Google Scholar] [CrossRef]
  201. Bossaert, S.; Crauwels, S.; Lievens, B.; De Rouck, G. The Power of Sour—A Review: Old Traditions, New Opportunities. BrewingScience 2019, 72, 78–88. [Google Scholar]
  202. Mahanta, S.; Sivakumar, P.S.; Parhi, P.; Mohapatra, R.K.; Dey, G.; Panda, S.H.; Sireswar, S.; Panda, S.K. Sour Beer Production in India Using a Coculture of Saccharomyces Pastorianus and Lactobacillus plantarum: Optimization, Microbiological, and Biochemical Profiling. Braz. J. Microbiol. 2022, 53, 947–958. [Google Scholar] [CrossRef]
  203. Cai, G.; Cao, Y.; Xiao, J.; Sheng, G.; Lu, J. The Mechanisms of Lactiplantibacillus plantarum J6-6 against Iso-α-Acid Stress and Its Application in Sour Beer Production. Syst. Microbiol. Biomanuf. 2024, 4, 1018–1027. [Google Scholar] [CrossRef]
  204. Nyhan, L.; Sahin, A.W.; Arendt, E.K. Co-Fermentation of Non-Saccharomyces Yeasts with Lactiplantibacillus plantarum FST 1.7 for the Production of Non-Alcoholic Beer. Eur. Food Res. Technol. 2023, 249, 167–181. [Google Scholar] [CrossRef]
  205. Zhu, Y.; Li, T.; Fu, X.; Abbasi, A.M.; Zheng, B.; Liu, R.H. Phenolics Content, Antioxidant and Antiproliferative Activities of Dehulled Highland Barley (Hordeum vulgare L.). J. Funct. Foods 2015, 19, 439–450. [Google Scholar] [CrossRef]
  206. Aron, P.M.; Shellhammer, T.H. A Discussion of Polyphenols in Beer Physical and Flavour Stability. J. Inst. Brew. 2010, 116, 369–380. [Google Scholar] [CrossRef]
  207. De Francesco, G.; Bravi, E.; Sanarica, E.; Marconi, O.; Cappelletti, F.; Perretti, G. Effect of Addition of Different Phenolic-Rich Extracts on Beer Flavour Stability. Foods 2020, 9, 1638. [Google Scholar] [CrossRef] [PubMed]
  208. Humia, B.V.; Santos, K.S.; Barbosa, A.M.; Sawata, M.; Mendonça, M.d.C.; Padilha, F.F. Beer Molecules and Its Sensory and Biological Properties: A Review. Molecules 2019, 24, 1568. [Google Scholar] [CrossRef]
  209. Domínguez-Tornay, A.; Díaz, A.B.; Lasanta, C.; Durán-Guerrero, E.; Castro, R. Co-Fermentation of Lactic Acid Bacteria and S. Cerevisiae for the Production of a Probiotic Beer: Survival and Sensory and Analytical Characterization. Food Biosci. 2024, 57, 103482. [Google Scholar] [CrossRef]
  210. Das, A.J.; Seth, D.; Miyaji, T.; Deka, S.C. Fermentation Optimization for a Probiotic Local Northeastern Indian Rice Beer and Application to Local Cassava and Plantain Beer Production. J. Inst. Brew. 2015, 121, 273–282. [Google Scholar] [CrossRef]
  211. Tang, F.; Wei, B.; Qin, C.; Huang, L.; Xia, N.; Teng, J. Enhancing the Inhibitory Activities of Polyphenols in Passion Fruit Peel on α-Amylase and α-Glucosidase via β-Glucosidase-Producing Lactobacillus Fermentation. Food Biosci. 2024, 62, 105005. [Google Scholar] [CrossRef]
  212. Dasenaki, M.E.; Thomaidis, N.S. Quality and Authenticity Control of Fruit Juices—A Review. Molecules 2019, 24, 1014. [Google Scholar] [CrossRef]
  213. Plessas, S. Advancements in the Use of Fermented Fruit Juices by Lactic Acid Bacteria as Functional Foods: Prospects and Challenges of Lactiplantibacillus (Lpb.) plantarum subsp. plantarum Application. Fermentation 2021, 8, 6. [Google Scholar] [CrossRef]
  214. Montet, D.; Ray, R.C.; Zakhia-Rozis, N. Lactic Acid Fermentation of Vegetables and Fruits. Microorg. Ferment. Tradit. Foods 2014, 21, 108–140. [Google Scholar]
  215. Yuan, X.; Wang, T.; Sun, L.; Qiao, Z.; Pan, H.; Zhong, Y.; Zhuang, Y. Recent Advances of Fermented Fruits: A Review on Strains, Fermentation Strategies, and Functional Activities. Food Chem. X 2024, 22, 101482. [Google Scholar] [CrossRef]
  216. Septembre-Malaterre, A.; Remize, F.; Poucheret, P. Fruits and Vegetables, as a Source of Nutritional Compounds and Phytochemicals: Changes in Bioactive Compounds during Lactic Fermentation. Food Res. Int. 2018, 104, 86–99. [Google Scholar] [CrossRef]
  217. Gustaw, K.; Niedźwiedź, I.; Rachwał, K.; Polak-Berecka, M. New Insight into Bacterial Interaction with the Matrix of Plant-Based Fermented Foods. Foods 2021, 10, 1603. [Google Scholar] [CrossRef]
  218. Sevindik, O.; Guclu, G.; Agirman, B.; Selli, S.; Kadiroglu, P.; Bordiga, M.; Capanoglu, E.; Kelebek, H. Impacts of Selected Lactic Acid Bacteria Strains on the Aroma and Bioactive Compositions of Fermented Gilaburu (Viburnum opulus) Juices. Food Chem. 2022, 378, 132079. [Google Scholar] [CrossRef]
  219. Di Cagno, R.; Coda, R.; De Angelis, M.; Gobbetti, M. Exploitation of Vegetables and Fruits through Lactic Acid Fermentation. Food Microbiol. 2013, 33, 1–10. [Google Scholar] [CrossRef] [PubMed]
  220. Filannino, P.; Di Cagno, R.; Gobbetti, M. Metabolic and Functional Paths of Lactic Acid Bacteria in Plant Foods: Get out of the Labyrinth. Curr. Opin. Biotechnol. 2018, 49, 64–72. [Google Scholar] [CrossRef]
  221. Tripathi, J.; Chatterjee, S.; Gamre, S.; Chattopadhyay, S.; Variyar, P.S.; Sharma, A. Analysis of Free and Bound Aroma Compounds of Pomegranate (Punica granatum L.). LWT-Food Sci. Technol. 2014, 59, 461–466. [Google Scholar] [CrossRef]
  222. Cele, N.P.; Akinola, S.A.; Manhivi, V.E.; Shoko, T.; Remize, F.; Sivakumar, D. Influence of Lactic Acid Bacterium Strains on Changes in Quality, Functional Compounds and Volatile Compounds of Mango Juice from Different Cultivars during Fermentation. Foods 2022, 11, 682. [Google Scholar] [CrossRef]
  223. Surendran, S.; Qassadi, F.; Surendran, G.; Lilley, D.; Heinrich, M. Myrcene—What Are the Potential Health Benefits of This Flavouring and Aroma Agent? Front. Nutr. 2021, 8, 699666. [Google Scholar] [CrossRef]
  224. Paventi, G.; de Acutis, L.; De Cristofaro, A.; Pistillo, M.; Germinara, G.S.; Rotundo, G. Biological Activity of Humulus lupulus (L.) Essential Oil and Its Main Components against Sitophilus granarius (L.). Biomolecules 2020, 10, 1108. [Google Scholar] [CrossRef] [PubMed]
  225. Sun, J.; Zhao, C.; Pu, X.; Li, T.; Shi, X.; Wang, B.; Cheng, W. Flavor and Functional Analysis of Lactobacillus plantarum Fermented Apricot Juice. Fermentation 2022, 8, 533. [Google Scholar] [CrossRef]
  226. Mrabti, H.N.; Jaouadi, I.; Zeouk, I.; Ghchime, R.; El Menyiy, N.; El Omari, N.; Balahbib, A.; Al-Mijalli, S.H.; Abdallah, E.M.; El-Shazly, M.; et al. Biological and Pharmacological Properties of Myrtenol: A Review. Curr. Pharm. Des. 2023, 29, 407–414. [Google Scholar] [CrossRef]
  227. Gao, H.; Wen, J.-J.; Hu, J.-L.; Nie, Q.-X.; Chen, H.-H.; Nie, S.-P.; Xiong, T.; Xie, M.-Y. Momordica Charantia Juice with Lactobacillus plantarum Fermentation: Chemical Composition, Antioxidant Properties and Aroma Profile. Food Biosci. 2019, 29, 62–72. [Google Scholar] [CrossRef]
  228. Ricci, A.; Cirlini, M.; Levante, A.; Dall’Asta, C.; Galaverna, G.; Lazzi, C. Volatile Profile of Elderberry Juice: Effect of Lactic Acid Fermentation Using L. plantarum, L. rhamnosus and L. casei Strains. Food Res. Int. 2018, 105, 412–422. [Google Scholar] [CrossRef]
  229. Di Cagno, R.; Surico, R.F.; Paradiso, A.; De Angelis, M.; Salmon, J.-C.; Buchin, S.; De Gara, L.; Gobbetti, M. Effect of Autochthonous Lactic Acid Bacteria Starters on Health-Promoting and Sensory Properties of Tomato Juices. Int. J. Food Microbiol. 2009, 128, 473–483. [Google Scholar] [CrossRef] [PubMed]
  230. Di Cagno, R.; Surico, R.F.; Minervini, G.; Rizzello, C.G.; Lovino, R.; Servili, M.; Taticchi, A.; Urbani, S.; Gobbetti, M. Exploitation of Sweet Cherry (Prunus avium L.) Puree Added of Stem Infusion through Fermentation by Selected Autochthonous Lactic Acid Bacteria. Food Microbiol. 2011, 28, 900–909. [Google Scholar] [CrossRef]
  231. Filannino, P.; Cardinali, G.; Rizzello, C.G.; Buchin, S.; De Angelis, M.; Gobbetti, M.; Di Cagno, R. Metabolic Responses of Lactobacillus plantarum Strains during Fermentation and Storage of Vegetable and Fruit Juices. Appl. Environ. Microbiol. 2014, 80, 2206–2215. [Google Scholar] [CrossRef]
  232. Hashemi, S.M.B.; Mousavi Khaneghah, A.; Barba, F.J.; Nemati, Z.; Sohrabi Shokofti, S.; Alizadeh, F. Fermented Sweet Lemon Juice (Citrus Limetta) Using Lactobacillus plantarum LS5: Chemical Composition, Antioxidant and Antibacterial Activities. J. Funct. Foods 2017, 38, 409–414. [Google Scholar] [CrossRef]
  233. Wang, H.; He, X.; Li, J.; Wu, J.; Jiang, S.; Xue, H.; Zhang, J.; Jha, R.; Wang, R. Lactic Acid Bacteria Fermentation Improves Physicochemical Properties, Bioactivity, and Metabolic Profiles of Opuntia Ficus-Indica Fruit Juice. Food Chem. 2024, 453, 139646. [Google Scholar] [CrossRef]
  234. Mashitoa, F.M.; Manhivi, V.E.; Akinola, S.A.; Garcia, C.; Remize, F.; Shoko, T.; Sivakumar, D. Changes in Phenolics and Antioxidant Capacity during Fermentation and Simulated in Vitro Digestion of Mango Puree Fermented with Different Lactic Acid Bacteria. J. Food Process Preserv. 2021, 45, e15937. [Google Scholar] [CrossRef]
  235. Chen, L.; Cao, H.; Huang, Q.; Xiao, J.; Teng, H. Absorption, Metabolism and Bioavailability of Flavonoids: A Review. Crit. Rev. Food Sci. Nutr. 2022, 62, 7730–7742. [Google Scholar] [CrossRef]
  236. Tang, S.; Cheng, Y.; Wu, T.; Hu, F.; Pan, S.; Xu, X. Effect of Lactobacillus plantarum-Fermented Mulberry Pomace on Antioxidant Properties and Fecal Microbial Community. LWT 2021, 147, 111651. [Google Scholar] [CrossRef]
  237. Hur, S.J.; Lee, S.Y.; Kim, Y.-C.; Choi, I.; Kim, G.-B. Effect of Fermentation on the Antioxidant Activity in Plant-Based Foods. Food Chem. 2014, 160, 346–356. [Google Scholar] [CrossRef]
  238. Slámová, K.; Kapešová, J.; Valentová, K. “Sweet Flavonoids”: Glycosidase-Catalyzed Modifications. Int. J. Mol. Sci. 2018, 19, 2126. [Google Scholar] [CrossRef]
  239. Gaur, G.; Gänzle, M.G. Conversion of (Poly)Phenolic Compounds in Food Fermentations by Lactic Acid Bacteria: Novel Insights into Metabolic Pathways and Functional Metabolites. Curr. Res. Food Sci. 2023, 6, 100448. [Google Scholar] [CrossRef] [PubMed]
  240. Meng, F.-B.; Lei, Y.-T.; Li, Q.-Z.; Li, Y.-C.; Deng, Y.; Liu, D.-Y. Effect of Lactobacillus plantarum and Lactobacillus Acidophilus Fermentation on Antioxidant Activity and Metabolomic Profiles of Loquat Juice. LWT 2022, 171, 114104. [Google Scholar] [CrossRef]
  241. Arunachalam, S.; Nagoor Meeran, M.F.; Azimullah, S.; Sharma, C.; Goyal, S.N.; Ojha, S. Nerolidol Attenuates Oxidative Stress, Inflammation, and Apoptosis by Modulating Nrf2/MAPK Signaling Pathways in Doxorubicin-Induced Acute Cardiotoxicity in Rats. Antioxid 2021, 10, 984. [Google Scholar] [CrossRef] [PubMed]
  242. Iqubal, A.; Syed, M.A.; Ali, J.; Najmi, A.K.; Haque, M.M.; Haque, S.E. Nerolidol Protects the Liver against Cyclophosphamide-Induced Hepatic Inflammation, Apoptosis, and Fibrosis via Modulation of Nrf2, NF-ΚB P65, and Caspase-3 Signaling Molecules in Swiss Albino Mice. Biofactors 2020, 46, 963–973. [Google Scholar] [CrossRef]
  243. Tang, W.; Xing, Z.; Li, C.; Wang, J.; Wang, Y. Molecular Mechanisms and in Vitro Antioxidant Effects of Lactobacillus plantarum MA2. Food Chem. 2017, 221, 1642–1649. [Google Scholar] [CrossRef]
  244. Li, Z.; Teng, J.; Lyu, Y.; Hu, X.; Zhao, Y.; Wang, M. Enhanced Antioxidant Activity for Apple Juice Fermented with Lactobacillus plantarum ATCC14917. Molecules 2018, 24, 51. [Google Scholar] [CrossRef]
  245. Chen, C.; Lu, Y.; Yu, H.; Chen, Z.; Tian, H. Influence of 4 Lactic Acid Bacteria on the Flavor Profile of Fermented Apple Juice. Food Biosci. 2019, 27, 30–36. [Google Scholar] [CrossRef]
  246. Peng, W.; Meng, D.; Yue, T.; Wang, Z.; Gao, Z. Effect of the Apple Cultivar on Cloudy Apple Juice Fermented by a Mixture of Lactobacillus Acidophilus, Lactobacillus plantarum, and Lactobacillus Fermentum. Food Chem. 2021, 340, 127922. [Google Scholar] [CrossRef]
  247. Hashemi, S.M.B.; Jafarpour, D. Fermentation of Bergamot Juice with Lactobacillus plantarum Strains in Pure and Mixed Fermentations: Chemical Composition, Antioxidant Activity and Sensorial Properties. LWT 2020, 131, 109803. [Google Scholar] [CrossRef]
  248. Tkacz, K.; Chmielewska, J.; Turkiewicz, I.P.; Nowicka, P.; Wojdyło, A. Dynamics of Changes in Organic Acids, Sugars and Phenolic Compounds and Antioxidant Activity of Sea Buckthorn and Sea Buckthorn-Apple Juices during Malolactic Fermentation. Food Chem. 2020, 332, 127382. [Google Scholar] [CrossRef] [PubMed]
  249. Filannino, P.; Cavoski, I.; Thlien, N.; Vincentini, O.; De Angelis, M.; Silano, M.; Gobbetti, M.; Di Cagno, R. Lactic Acid Fermentation of Cactus Cladodes (Opuntia ficus-indica L.) Generates Flavonoid Derivatives with Antioxidant and Anti-Inflammatory Properties. PLoS ONE 2016, 11, e0152575. [Google Scholar] [CrossRef]
  250. Wang, J.; Wei, B.-C.; Wang, X.; Zhang, Y.; Gong, Y.-J. Aroma Profiles of Sweet Cherry Juice Fermented by Different Lactic Acid Bacteria Determined through Integrated Analysis of Electronic Nose and Gas Chromatography–Ion Mobility Spectrometry. Front. Microbiol. 2023, 14, 1113594. [Google Scholar] [CrossRef]
  251. Kuerban, D.; Lu, J.; Huangfu, Z.; Wang, L.; Qin, Y.; Zhang, M. Optimization of Fermentation Conditions and Metabolite Profiling of Grape Juice Fermented with Lactic Acid Bacteria for Improved Flavor and Bioactivity. Foods 2023, 12, 2407. [Google Scholar] [CrossRef]
  252. Huang, Y.; Wang, H.; Zhu, C. Effect of Lactic Acid Bacteria Fermentation on Antioxidation and Bioactivity of Hawthorn Pulp. IOP Conf. Ser. Earth Environ. Sci. 2019, 267, 062056. [Google Scholar] [CrossRef]
  253. Pan, X.; Zhang, S.; Xu, X.; Lao, F.; Wu, J. Volatile and Non-Volatile Profiles in Jujube Pulp Co-Fermented with Lactic Acid Bacteria. LWT 2022, 154, 112772. [Google Scholar] [CrossRef]
  254. Li, T.; Jiang, T.; Liu, N.; Wu, C.; Xu, H.; Lei, H. Biotransformation of Phenolic Profiles and Improvement of Antioxidant Capacities in Jujube Juice by Select Lactic Acid Bacteria. Food Chem. 2021, 339, 127859. [Google Scholar] [CrossRef] [PubMed]
  255. Zhao, M.; Zhang, F.; Zhang, L.; Liu, B.; Meng, X. Mixed Fermentation of Jujube Juice (Ziziphus jujuba Mill.) with L. rhamnosus GG and L. plantarum-1: Effects on the Quality and Stability. Int. J. Food Sci. Technol. 2019, 54, 2624–2631. [Google Scholar] [CrossRef]
  256. Wang, D.; Deng, Y.; Chen, X.; Wang, K.; Zhao, L.; Wang, Z.; Liu, X.; Hu, Z. Elucidating the Effects of Lactobacillus plantarum Fermentation on the Aroma Profiles of Pasteurized Litchi Juice Using Multi-Scale Molecular Sensory Science. Curr. Res. Food Sci. 2023, 6, 100481. [Google Scholar] [CrossRef]
  257. Liu, S.; Peng, Y.-J.; He, W.-W.; Song, X.-X.; He, Y.-X.; Hu, X.-Y.; Bian, S.-G.; Li, Y.-H.; Yin, J.-Y.; Nie, S.-P.; et al. Metabolomics-Based Mechanistic Insights into Antioxidant Enhancement in Mango Juice Fermented by Various Lactic Acid Bacteria. Food Chem. 2025, 466, 142078. [Google Scholar] [CrossRef]
  258. Park, J.B.; Lim, S.H.; Sim, H.S.; Park, J.H.; Kwon, H.J.; Nam, H.S.; Kim, M.D.; Baek, H.H.; Ha, S.J. Changes in Antioxidant Activities and Volatile Compounds of Mixed Berry Juice through Fermentation by Lactic Acid Bacteria. Food Sci. Biotechnol. 2017, 26, 441–446. [Google Scholar] [CrossRef] [PubMed]
  259. Kwaw, E.; Ma, Y.; Tchabo, W.; Apaliya, M.T.; Wu, M.; Sackey, A.S.; Xiao, L.; Tahir, H.E. Effect of Lactobacillus Strains on Phenolic Profile, Color Attributes and Antioxidant Activities of Lactic-Acid-Fermented Mulberry Juice. Food Chem. 2018, 250, 148–154. [Google Scholar] [CrossRef]
  260. Yaqoob, S.; Imtiaz, A.; Awan, K.A.; Murtaza, M.S.; Mubeen, B.; Yinka, A.A.; Boasiako, T.A.; Alsulami, T.; Rehman, A.; Khalifa, I.; et al. Impact of Fermentation through Synergistic Effect of Different Lactic Acid Bacteria (Mono and Co-Cultures) on Metabolic and Sensorial Profile of Mulberry Juice. J. Food Meas. Charact. 2024, 18, 9364–9384. [Google Scholar] [CrossRef]
  261. de la Fuente, B.; Luz, C.; Puchol, C.; Meca, G.; Barba, F.J. Evaluation of Fermentation Assisted by Lactobacillus Brevis POM, and Lactobacillus plantarum (TR-7, TR-71, TR-14) on Antioxidant Compounds and Organic Acids of an Orange Juice-Milk Based Beverage. Food Chem. 2021, 343, 128414. [Google Scholar] [CrossRef]
  262. Dogan, K.; Akman, P.K.; Tornuk, F. Role of Non-thermal Treatments and Fermentation with Probiotic Lactobacillus plantarum on in Vitro Bioaccessibility of Bioactives from Vegetable Juice. J. Sci. Food Agric. 2021, 101, 4779–4788. [Google Scholar] [CrossRef]
  263. Fonseca, H.C.; Melo, D.d.S.; Ramos, C.L.; Dias, D.R.; Schwan, R.F. Lactiplantibacillus plantarum CCMA 0743 and Lacticaseibacillus Paracasei Subsp. Paracasei LBC-81 Metabolism during the Single and Mixed Fermentation of Tropical Fruit Juices. Braz. J. Microbiol. 2021, 52, 2307–2317. [Google Scholar] [CrossRef] [PubMed]
  264. Mantzourani, I.; Kazakos, S.; Terpou, A.; Alexopoulos, A.; Bezirtzoglou, E.; Bekatorou, A.; Plessas, S. Potential of the Probiotic Lactobacillus plantarum ATCC 14917 Strain to Produce Functional Fermented Pomegranate Juice. Foods 2019, 8, 4. [Google Scholar] [CrossRef]
  265. Vivek, K.; Mishra, S.; Pradhan, R.C.; Jayabalan, R. Effect of Probiotification with Lactobacillus plantarum MCC 2974 on Quality of Sohiong Juice. LWT 2019, 108, 55–60. [Google Scholar] [CrossRef]
  266. Liu, S.; He, Y.; He, W.; Song, X.; Peng, Y.; Hu, X.; Bian, S.; Li, Y.; Nie, S.; Yin, J.; et al. Exploring the Biogenic Transformation Mechanism of Polyphenols by Lactobacillus plantarum NCU137 Fermentation and Its Enhancement of Antioxidant Properties in Wolfberry Juice. J. Agric. Food Chem. 2024, 72, 12752–12761. [Google Scholar] [CrossRef]
  267. Tian, Y.; Wang, Y.; Zhang, N.; Xiao, M.; Zhang, J.; Xing, X.; Zhang, Y.; Fan, Y.; Li, X.; Nan, B.; et al. Antioxidant Mechanism of Lactiplantibacillus plantarum KM1 Under H2O2 Stress by Proteomics Analysis. Front. Microbiol. 2022, 13, 897387. [Google Scholar] [CrossRef]
  268. Markkinen, N.; Laaksonen, O.; Nahku, R.; Kuldjärv, R.; Yang, B. Impact of Lactic Acid Fermentation on Acids, Sugars, and Phenolic Compounds in Black Chokeberry and Sea Buckthorn Juices. Food Chem. 2019, 286, 204–215. [Google Scholar] [CrossRef] [PubMed]
  269. Wei, M.; Wang, S.; Gu, P.; Ouyang, X.; Liu, S.; Li, Y.; Zhang, B.; Zhu, B. Comparison of Physicochemical Indexes, Amino Acids, Phenolic Compounds and Volatile Compounds in Bog Bilberry Juice Fermented by Lactobacillus plantarum under Different pH Conditions. J. Food Sci. Technol. 2018, 55, 2240–2250. [Google Scholar] [CrossRef] [PubMed]
  270. Yilmaz, B.; Bangar, S.P.; Echegaray, N.; Suri, S.; Tomasevic, I.; Lorenzo, J.M.; Melekoglu, E.; Rocha, J.M.; Ozogul, F. The Impacts of Lactiplantibacillus plantarum on the Functional Properties of Fermented Foods: A Review of Current Knowledge. Microorganisms 2022, 10, 826. [Google Scholar] [CrossRef] [PubMed]
Figure 1. Release of free aroma compounds from glycosidically bound precursors by β-glucosidase activity. Representation of enzymatic activities involved in the release of the volatile aglycone component from three different disaccharide-bound aroma compounds.
Figure 1. Release of free aroma compounds from glycosidically bound precursors by β-glucosidase activity. Representation of enzymatic activities involved in the release of the volatile aglycone component from three different disaccharide-bound aroma compounds.
Foods 14 01451 g001
Figure 2. Release of free isoflavone from the three main soy isoflavones glycosides and their acetylated/malonylated forms. Representation of the two-step process by which the acetyl- and malonyl-forms of soy-glycosylated isofavones (daidzin, glycystin, and genistin) are hydrolyzed by esterase and β-glucosidase to release the free form of isoflavone (daidzein, glycistein, and genistein).
Figure 2. Release of free isoflavone from the three main soy isoflavones glycosides and their acetylated/malonylated forms. Representation of the two-step process by which the acetyl- and malonyl-forms of soy-glycosylated isofavones (daidzin, glycystin, and genistin) are hydrolyzed by esterase and β-glucosidase to release the free form of isoflavone (daidzein, glycistein, and genistein).
Foods 14 01451 g002
Figure 3. Cyanidric acid generation by cyanogenic glycosides present in cassava tissues. Degradation of the two principal cyanogenic glycosides (limarin and lotaustralin) of cassava by β-glucosidase activity with production of glucose and subsequent release of cyanidric acid. Targets of this high toxic compound are haemoglobin of erythocytes and cytochrome c oxidase, the complex IV (in red) of the respiratory chain embedded in the inner membrane of the mitochondrion. Abbreviations: m.o.m., mitochondrial outer membrane; i.s., intermembrane space; m.i.m., mitochondrial inner membrane.
Figure 3. Cyanidric acid generation by cyanogenic glycosides present in cassava tissues. Degradation of the two principal cyanogenic glycosides (limarin and lotaustralin) of cassava by β-glucosidase activity with production of glucose and subsequent release of cyanidric acid. Targets of this high toxic compound are haemoglobin of erythocytes and cytochrome c oxidase, the complex IV (in red) of the respiratory chain embedded in the inner membrane of the mitochondrion. Abbreviations: m.o.m., mitochondrial outer membrane; i.s., intermembrane space; m.i.m., mitochondrial inner membrane.
Foods 14 01451 g003
Table 1. Main effects of the β-glucosidase activity in plant-based products fermented by some LAB and bifidobacteria.
Table 1. Main effects of the β-glucosidase activity in plant-based products fermented by some LAB and bifidobacteria.
FoodLAB Speciesβ-Glucosidase FunctionRefs.
soybean
products
Lactococcus lactis
Lacticaseibacillus casei
Limosilactobacillus fermentum
Limosilactobacillus mucosae
Enterococcus faecalis
L. plantarum
Lacticaseibacillus rhamnosus Bifidobacterium pseudocatenulatum
Bifidobacterium breve
deglycosylation of isoflavones (genistin, daidzin, and glycitin)[77,78,79,80,81]
oliveL. plantarum
L. casei
Lacticaseibacillus paracasei
Bifidobacterium lactis
Enterococcus faecium
Lactiplantibacillus pentosus
debittering (hydrolysis of the oleuropein)[82,83,84,85,86,87]
alcoholic beverages
(wine and beer)
Oenococcus oeni
Pediococcus spp.
L. plantarum
deglycosylation of flavor precursors with release of free volatile organic compounds[88,89,90,91,92,93,94]
non-alcoholic fermented fruitL. rhamnosus
L. plantarum
Leuconostoc mesenteroides
Levilactobacillus brevis
Bifidobacterium spp.
deglycosylation of flavor precursors with release of free volatile organic compounds[82,95,96,97]
cassavaL. plantarum
L. mesenteroides
hydrolysis of cyanogenic glycosides (linamarin)[98,99,100,101]
Table 2. Main positive effects potentially related to β-glucosidase activity of L. plantarum in fermented fruit.
Table 2. Main positive effects potentially related to β-glucosidase activity of L. plantarum in fermented fruit.
Fruit ProcessedProduct TypeL. plantarum (Lp) StrainsMain Positive EffectsRef.
AppleJuice fermented at 37 °C for 72 h.Lp ATCC14917Increased antioxidant activity and decreased total phenolics and flavonoid content.[244]
AppleJuice fermented at 37 °C for 80 hLp ST-IIIImproved flavor profile[245]
AppleSingle juices from nine apple cultivars fermented at 37 °C for 24 hLp CICC21805Increased terpenes D-limonene and eugenol in some apple cultivars[246]
ApricotJuice fermented at 37 °C for 12 hLp LP56Increased antioxidant activity and total phenolics; improved flavor profile[225]
Bergamot (Citrus Bergamia Risso)Juice fermented at 37 °C for 72 hSingle and mixed starter:
Lp PTCC 1896
Lp AF1
Lp LP3
Increased antioxidant activity[247]
Buckthorn berries
(Hippophaë rhamnoides L.)
Juice fermented at 30 °C for 72 hLp DSM 10492
Lp DSM 20174
Lp DSM 6872
Increased antioxidant activity and flavonoids[248]
Cactus (Opuntia ficus-indica L.)Cladodes pulp fermented at 30 °C for 24 hSingle starters:
Lp CIL6
Lp POM1
Lp 1MR20
Increased antioxidant activity and flavonoids (kaemferol and isorhamnetin)[249]
Cherries (Prunus avium L.)Juice fermented at 37 °C for 48 hLp JYLP-375Improved flavor profile[250]
Cranberrybush/Gilaburu (Viburnum opulus L.)Juice fermented at 30 °C for 12 daysLp-23Increased antioxidant activity and terpenes[218]
Elderberry (Sambucus nigra L.)Juice fermented at 37 °C for 48 hSingle starters:
Lp POM1
Lp 1LE1
Lp C1
Lp 1486
Lp 285
Increase in terpenes and norisoprenoids (limonene, β-linalool, β-damascenone, and eugenol)[228]
GrapesJuice fermented at 37 °C for 32 hSingle and mixed starter:
Lp 90
L. casei
Increased total phenolics and improved flavor profile[251]
Hawthorn (Crataegus pinnatifida)Pulp fermented at 37 °C for 12 hMixed starter: Lp, Lactobacillus acidophilus and L. caseiIncreased total phenolics and flavonoids[252]
Jujube (Ziziphus jujuba Milll.)Pulp fermented at 37 °C for 24 hLp CICC 20265Improved flavor profile[253]
Jujube (Zizyphus jujuba Mill.)Juice fermented at 37 °C for 48 hLp 90Increased antioxidant activity and flavor profile[254]
Jujube (Ziziphus jujuba Milll.)Juice fermented at 37 °C for 28 hSingle and mixed starter:
L. rhamnosus GG
Lp-1
Lp-2
L. paracasei 22709
Leuconostoc mesenteroides 22264
Decreased total phenolics and increased total flavonoid content;
improved flavor profile
[255]
Lemon (Citrus limetta)Juice fermented at 37 °C for 48 hLp LS5Increased antioxidant activity[232]
Litchi (Litchi chinensis Sonn.Juice fermented at 37 °C for 40 hSingle starters:
Lp LP28
Lp LP226
Lp LPC2W
Increased terpenes citronellol, linalool, geraniol, and prenol[256]
Loquat (Eriobotrya japonica Lindl.)Juice fermented at 36 °C for 48 hLp LZ 2-2Increased antioxidant activity, total phenolics, and total flavonoids[240]
Mango (Mangifera indica L.)Juice fermented at 37 °C for 48 hLp NCU116Increased antioxidant activity and total phenolics[257]
Mango (Mangifera indica L.)Juice fermented at 30 °C for 72 hSingle and mixed starter
Lp L75
Leuconostoc pseudomesenteroides L 56
Increased antioxidant activity and improved flavor profile[222]
Mixed berry (acai berry, aronia, cranberry)Juice fermented at 37 °C for 36 hLp LP-115Increased antioxidant activity[258]
Momordica charantia L.Juice fermented at 37 °C for 48 hLp NCU116Increased antioxidant activity, total phenolics, and total flavonoids[227]
Mulberry
(Morus nigra)
Juice fermented at 37 °C for 36 hLp ATCC SD5209Increased antioxidant activity and phenolics (phenolic acids, anthocyanins, and flavonols)[259]
Mulberry
(Morus nigra)
Juice fermented at 37 °C for 7 daysLp CICC 20265Increased antioxidant activity[236]
Mulberry
(Morus nigra)
Juice fermented at 37 °C for 48 hLp (single colture and/or in co-colture with other LAB)Improvement of both nutritional and aromatic profile[260]
OrangeJuice-milk fermented at 37 °C for 72 hSingle starters:
Lp TR-7
Lp TR-71
Lp TR-14
Increased antioxidant activity and total phenolics[261]
Orange, lemon, celery and carrotMixed vegetable juice fermented at 37 °C for 24 hLp HFC8Increased antioxidant activity and phenolics (flavonoids and anthocyanins)[262]
Passion fruit (Passiflora edulis), acerola (Malpighia emarginata), and jelly palm (Butia capitata)Juice fermented at 37 °C for 24 hLp CCMA 0743Increased flavonoids[263]
Pomegranate (Punica granatum L.)Juice fermented at 30 °C for 24 hLp ATCC 14917Increased antioxidant activity and total phenolics[264]
Pomegranate (Punica granatum L.)Juice fermented at 30 °C for 120 hSingle starter:
Lp C2
Lp POM1
Improved flavor profile[97]
Sohiong (Prunus nepalensis)Juice fermented at 37 °C for 72 hLp MCC 297Increased antioxidant activity, total phenolics, and anthocyanins[265]
WolfberryJuice fermented at 37 °C for 48 hLp NCU137Increased antioxidant activity and free phenolics[266]
Disclaimer/Publisher’s Note: The statements, opinions and data contained in all publications are solely those of the individual author(s) and contributor(s) and not of MDPI and/or the editor(s). MDPI and/or the editor(s) disclaim responsibility for any injury to people or property resulting from any ideas, methods, instructions or products referred to in the content.

Share and Cite

MDPI and ACS Style

Paventi, G.; Di Martino, C.; Coppola, F.; Iorizzo, M. β-Glucosidase Activity of Lactiplantibacillus plantarum: A Key Player in Food Fermentation and Human Health. Foods 2025, 14, 1451. https://doi.org/10.3390/foods14091451

AMA Style

Paventi G, Di Martino C, Coppola F, Iorizzo M. β-Glucosidase Activity of Lactiplantibacillus plantarum: A Key Player in Food Fermentation and Human Health. Foods. 2025; 14(9):1451. https://doi.org/10.3390/foods14091451

Chicago/Turabian Style

Paventi, Gianluca, Catello Di Martino, Francesca Coppola, and Massimo Iorizzo. 2025. "β-Glucosidase Activity of Lactiplantibacillus plantarum: A Key Player in Food Fermentation and Human Health" Foods 14, no. 9: 1451. https://doi.org/10.3390/foods14091451

APA Style

Paventi, G., Di Martino, C., Coppola, F., & Iorizzo, M. (2025). β-Glucosidase Activity of Lactiplantibacillus plantarum: A Key Player in Food Fermentation and Human Health. Foods, 14(9), 1451. https://doi.org/10.3390/foods14091451

Note that from the first issue of 2016, this journal uses article numbers instead of page numbers. See further details here.

Article Metrics

Back to TopTop