Search Results (17)

Multiple sclerosis (MS) is a neurodegenerative disease, with inflammation and oxidative stress in the central nervous system being the main triggers. There are many drugs that reduce the clinical signs of MS, but none of them cure the disease. Food proteins have been shown to contain encrypted peptides that can be released after hydrolysis and exert numerous biological activities. Recently, we have demonstrated the anti-inflammatory and antioxidant activities of a lupin protein hydrolysate (LPH) both in vitro and in vivo. Therefore, the aim of this study was to evaluate whether LPH is capable of reducing the clinical signs of experimental autoimmune encephalomyelitis (EAE), a mouse model of MS. EAE was induced in female C57BL/6N mice and they were treated intragastrically with LPH (100 mg/kg) or vehicle (control group) from day 0 (prophylactic approach) or from the onset of the disease (day 12 post-induction; therapeutic approach) and the clinical score of each mouse was recorded daily. Prophylactic treatment with LPH reduced the clinical score of the mice compared to the control group, as well as the maximum and cumulative scores, without changing the day of onset of the symptoms while the therapeutic intervention did not significantly improve the severity of the disease. For the first time, we demonstrated that prophylactic administration of LPH reduces the severity of MS, suggesting a potential nutraceutical or new functional foods in neuroinflammation. However, further studies are needed to confirm this nutritional effect in a clinical context. Full article

We investigated the effect of feed deprivation for 45 days on the growth, immunity, and health of 0⁺marron (Cherax cainii) initially fed for 110 days on various protein sources including fishmeal (FM), poultry by-product meal (PBM), black soldier fly meal (BSFM), soybean meal (SBM), lupin meal (LM), and tuna hydrolysate. The marron were weighed and sacrificed immediately after feeding stopped (day 0) and at days 15, 30, and 45 after the feed deprivation trial commenced. Total haemolymph count, differential haemocyte count, lysozyme activity, protease activity, total bacterial count in the digestive tract, and organosomatic indices were analysed. Initially feeding marron any protein sources did not influence the percentage of weight gain and specific growth rates of marron. All marron showed more than 83% survival; however, marron fed soybean meal showed significantly lower survival than others. Dietary sources of protein altered organosomatic indices of starved marron during various starvation periods and resulted in a significant decrease in total haemocyte counts, lysozyme activity, protease activity, and bacterial count in the digestive tract of marron. Starved marron initially fed PBM and BSFM showed higher tolerance to starvation, followed by marron initially fed FM and SBM, while marron initially fed TH and LM showed the highest susceptibility to starvation. Full article

Lupin (Lupinus angustifolius L.) proteins are potential sources of bioactive peptides (LBPs) that can inhibit dipeptidyl peptidase IV (DPP-IV) and angiotensin I-converting enzyme (ACE-I) activity. However, the capacity of different enzymes to release LBPs, the pharmacokinetic and bioactivities of the peptides released, and their binding affinities with the active sites of DPP-IV and ECA-I are topics scarcely addressed. Therefore, we used in silico hydrolysis (BIOPEP-UWM platform) with various enzymes to predict the release of LBPs. Among the bioactive peptides identified in lupin proteins (n = 4813), 2062 and 1558 had DPP-IV and ACE-I inhibitory activity, respectively. Ficin, bromelain, and papain released the highest proportion of ACE-I (n = 433, 411, and 379, respectively) and DPP-IV (n = 556, 544, and 596, respectively) inhibitory peptides. LBPs with favorable pharmacokinetics and gastrointestinal stability tightly interacted with the active sites of ACE-I (–5.6 to –8.9 kcal/mol) and DPP-IV (–5.4 to –7.6 kcal/mol). Papain generated the most bioavailable LBPs (n = 459) with ACE-I (n = 223) and DPP-IV (n = 412) inhibitory activity. These peptides were non-toxic and gastrointestinal digestion stable. Notably, papain-based hydrolysis released some LBPs (n = 270) that inhibited both ACE-I and DPP-IV. Plant protease-based hydrolysis is a promising approach for producing lupin hydrolysates with ACE-I and DPP-IV inhibitory activities. Full article

This study investigates the production of protein hydrolysates with dipeptidyl peptidase-IV (DPP-IV) inhibitory activity from agro-industrial by-products, namely olive seed, sunflower seed, rapeseed, and lupin meals, as well as from two plant protein isolates such as pea and potato. Furthermore, the effect of simulated gastrointestinal digestion on the DPP-IV inhibitory activity of all the hydrolysates was evaluated. Overall, the lowest values of IC₅₀ (1.02 ± 0.09 – 1.24 ± 0.19 mg protein/mL) were observed for the hydrolysates with a high proportion of short-chain [< 1 kDa] peptides (i.e., olive seed, sunflower seed, and lupin) or high content of proline (i.e., rapeseed). Contrarily, the IC₅₀ of the pea and potato hydrolysates was significantly higher (1.50 ± 0.13 – 1.93 ± 0.13 mg protein/mL). In vitro digestion led to an increase in peptides <1 kDa for almost all hydrolysates (except olive and sunflower seed meals), which was noticeable for rapeseed, pea, and potato hydrolysates. Digestion did not significantly modify the DPP-IV inhibitory activity of olive, sunflower, rapeseed, and potato hydrolysates, whereas a significant decrease in IC₅₀ value was obtained for pea hydrolysate and a significant increase in IC₅₀ was obtained for lupin hydrolysate. Thus, this work shows the potential of agro-industrial by-products for the production of protein hydrolysates exhibiting DPP-IV inhibition. Full article

Although its high protein content, bioactive compounds, and dietary fibers have many health benefits, lupine (Lupinus sp.) was undervalued as a resourceful plant. In the last years, however, the number of studies on the use of lupine as a potential food ingredient has increased. In this study, obtaining a sweet lupine protein concentrate (SLPC) hydrolysate with a high degree of hydrolysis (DH) and a simultaneous low intensity of bitterness was pursued. The experimental design was carried out, according to Taguchi methodology, using three experimental parameters: enzyme concentration (0.5–1.5%), temperature (50–60 °C), and time (1–4 h), with three levels each. The optimal conditions for the enzymatic hydrolysis process of SLPC with Alcalase 2.4 L were enzyme concentration 1.5%, temperature 50 °C, and time 4 h, for which the best DH, 41.96%, was achieved. The SLPC hydrolysate as a food ingredient was characterized in terms of DH, bitter taste intensity, amino acid profile, and techno-functional properties. The results showed an increase of water binding capacity to 1.45 g/g, emulsification activity of 50.91%, and 92% stability of the emulsion, while the evaluated intensity of bitterness was 4.6 on a 7- point scale. Based on its technological, functional, sensory, and chemical characteristics, this study recommends the use of SLPC hydrolysate as a food ingredient in various food matrices. Full article

Solubility and emulsifying properties are important functional properties associated with proteins. However, many plant proteins have lower techno-functional properties, which limit their functional performance in many formulations. Therefore, the objective of this study was to investigate the effect of protein hydrolysis by commercial enzymes to improve their solubility and emulsifying properties. Lupin protein isolate (LPI) was hydrolyzed by 7 commercial proteases using different E/S ratios and hydrolysis times while the solubility and emulsifying properties were evaluated. The results showed that neutral and alkaline proteases are most efficient in hydrolyzing lupin proteins than acidic proteases. Among the proteases, Protamex^® (alkaline protease) showed the highest DH values after 5 h of protein hydrolysis. Meanwhile, protein solubility of LPI hydrolysates was significantly higher (p < 0.05) than untreated LPI at all pH analyzed values. Moreover, the emulsifying capacity (EC) of undigested LPI was lower than most of the hydrolysates, except for acidic proteases, while emulsifying stability (ES) was significantly higher (p < 0.05) than most LPI hydrolysates by acidic proteases, except for LPI hydrolyzed with Acid Stable Protease with an E/S ratio of 0.04. In conclusion, the solubility, and emulsifying properties of lupin (Lupinus luteus) proteins can be improved by enzymatic hydrolysis using commercial enzymes. Full article

Dietary proteins are no longer just nutritional ingredients in our food. During hydrolysis, some of the released peptides may possess properties that favor the health of the human body. In our study enzymatic hydrolysis of lupin proteins was performed using papain. Three enzyme-to-substrate ratios were set for three different duration times. The SDS-PAGE of the samples was performed. Each hydrolysate was studied for the degree of hydrolysis (DH), acetylcholinesterase (AChE) inhibitory, antimicrobial, and antioxidant activities (AOA, according to four spectrophotometric methods). The DH varied from 9.06 ± 0.20 to 27.97 ± 0.37%. According to the results, the best AOA was measured by the ABTS method (from 0.76 ± 0.03 to 1.15 ± 0.46 M TE/100 g protein). All the hydrolysates displayed AChE inhibitory activity (IC50), which varied between 155.58 ± 1.87 and 199.63 ± 0.41 mg/g protein. To the best of our knowledge, this is the first report of the acetylcholinesterase inhibitory activity of lupin protein hydrolysates. In conclusion, lupin proteins prove to have a high potential to serve as a source of bioactive peptides. Full article

The use of natural ingredients for managing diabetes is becoming more popular in recent times due to the several adverse effects associated with synthetic antidiabetic medications. In this study, we investigated the in vitro antidiabetic potential (through inhibition of α-glucosidase (AG) and α-amylase (AA)) of hydrolysates from lupin proteins pretreated with ultrasound and hydrolyzed using alcalase (ACT) and flavourzyme (FCT). We further fractionated ACT and FCT into three molecular weight fractions. Unfractionated ACT and FCT showed significantly (p < 0.05) higher AG (IC₅₀ value = 1.65 mg/mL and 1.91 mg/mL) and AA (IC₅₀ value = 1.66 mg/mL and 1.98 mg/mL) inhibitory activities than their ultrafiltrated fractions, where lower IC₅₀ values indicate higher inhibitory activities. Then, ACT and FCT were subjected to peptide sequencing using LC-MS-QTOF to identify the potential AG and AA inhibitors. Molecular docking was performed on peptides with the highest number of hotspots and PeptideRanker score to study their interactions with AG and AA enzymes. Among the peptides identified, SPRRF, FE, and RR were predicted to be the most active peptides against AG, while AA inhibitors were predicted to be RPR, PPGIP, and LRP. Overall, hydrolysates prepared from lupin proteins using alcalase and flavourzyme may be useful in formulating functional food for managing diabetics. Full article

Anxiety is the most prevalent psychiatric disorder worldwide, causing a substantial economic burden due to the associated healthcare costs. Given that commercial anxiolytic treatments may cause important side effects and have medical restrictions for prescription and high costs, the search for new natural and safer treatments is gaining attention. Since lupin protein hydrolysate (LPH) has been shown to be safe and exert anti-inflammatory and antioxidant effects, key risk factors for the anxiety process and memory impairment, we evaluated in this study the potential effects of LPH on anxiety and spatial memory in a Western diet (WD)-induced anxiety model in ApoE^−/− mice. We showed that 20.86% of the 278 identified LPH peptides have biological activity related to anxiolytic/analgesic effects; the principal motifs found were the following: VPL, PGP, YL, and GQ. Moreover, 14 weeks of intragastrical LPH treatment (100 mg/kg) restored the WD-induced anxiety effects, reestablishing the anxiety levels observed in the standard diet (SD)-fed mice since they spent less time in the anxiety zones of the elevated plus maze (EPM). Furthermore, a significant increase in the number of head dips was recorded in LPH-treated mice, which indicates a greater exploration capacity and less fear due to lower levels of anxiety. Interestingly, the LPH group showed similar thigmotaxis, a well-established indicator of animal anxiety and fear, to the SD group, counteracting the WD effect. This is the first study to show that LPH treatment has anxiolytic effects, pointing to LPH as a potential component of future nutritional therapies in patients with anxiety. Full article

In this work, we evaluated the physical and oxidative stabilities of 5% w/w fish oil-in-water emulsions stabilized with 1%wt Tween20 and containing 2 mg/mL of protein hydrolysates from olive seed (OSM–H), sunflower (SFSM–H), rapeseed (RSM–H) and lupin (LUM–H) meals. To this end, the plant-based substrates were hydrolyzed at a 20% degree of hydrolysis (DH) employing a mixture 1:1 of subtilisin: trypsin. The hydrolysates were characterized in terms of molecular weight profile and in vitro antioxidant activities (i.e., DPPH scavenging and ferrous ion chelation). After incorporation of the plant protein hydrolysates as water-soluble antioxidants in the emulsions, a 14-day storage study was conducted to evaluate both the physical (i.e., ζ-potential, droplet size and emulsion stability index) and oxidative (e.g., peroxide and anisidine value) stabilities. The highest in vitro DPPH scavenging and iron (II)-chelating activities were exhibited by SFSM–H (IC₅₀ = 0.05 ± 0.01 mg/mL) and RSM–H (IC₅₀ = 0.41 ± 0.06 mg/mL). All the emulsions were physically stable within the storage period, with ζ-potential values below −35 mV and an average mean diameter D[4,3] of 0.411 ± 0.010 μm. Although LUM–H did not prevent lipid oxidation in emulsions, OSM–H and SFSM–H exhibited a remarkable ability to retard the formation of primary and secondary lipid oxidation products during storage when compared with the control emulsion without antioxidants. Overall, our findings show that plant-based enzymatic hydrolysates are an interesting alternative to be employed as natural antioxidants to retard lipid oxidation in food emulsions. Full article

Agri-food industries generate several by-products, including protein-rich materials currently treated as waste. Lupine species could be a sustainable alternative source of protein compared to other crops such as soybean or chickpea. Protein hydrolysates contain bioactive peptides that may act positively in disease prevention or treatment. Inflammatory responses and oxidative stress underlie many chronic pathologies and natural treatment approaches have gained attention as an alternative to synthetic pharmaceuticals. Recent studies have shown that lupin protein hydrolysates (LPHs) could be an important source of biopeptides, especially since they demonstrate anti-inflammatory properties. However, due to their possible degradation by digestive and brush-border enzymes, it is not clear whether these peptides can resist intestinal absorption and reach the bloodstream, where they may exert their biological effects. In this work, the in vitro cellular uptake/transport and the anti-inflammatory and antioxidant properties of LPH were investigated in a co-culture system with intestinal epithelial Caco-2 cells and THP-1-derived macrophages. The results indicate that the LPH crosses the human intestinal Caco-2 monolayer and exerts anti-inflammatory activity in macrophages located in the basement area by decreasing mRNA levels and the production of pro-inflammatory cytokines. A remarkable reduction in nitric oxide and ROS in the cell-based system by peptides from LPH was also demonstrated. Our preliminary results point to underexplored protein hydrolysates from food production industries as a novel, natural source of high-value-added biopeptides. Full article

There is a renewed interest on the reliance of food-based bioactive compounds as sources of nutritive factors and health-beneficial chemical compounds. Among these food components, several proteins from foods have been shown to promote health and wellness as seen in proteins such as α/γ-conglutins from the seeds of Lupinus species (Lupin), a genus of leguminous plant that are widely used in traditional medicine for treating chronic diseases. Lupin-derived peptides (LDPs) are increasingly being explored and they have been shown to possess multifunctional health improving properties. This paper discusses the intestinal transport, bioavailability and biological activities of LDPs, focusing on molecular mechanisms of action as reported in in vitro, cell culture, animal and human studies. The potentials of several LDPs to demonstrate multitarget mechanism of regulation of glucose and lipid metabolism, chemo- and osteoprotective properties, and antioxidant and anti-inflammatory activities position LDPs as good candidates for nutraceutical development for the prevention and management of medical conditions whose etiology are multifactorial. Full article

Metabolic-associated fatty liver disease (MAFLD) is the most important cause of liver disease worldwide. It is characterized by the accumulation of fat in the liver and is closely associated with abdominal obesity. In addition, oxidative stress and inflammation are significant features involved in MAFLD. Recently, our group demonstrated that lupin protein hydrolysates (LPHs) had lipid lowering, antioxidant, and anti-inflammatory effects. Sixty male mice fed with a Western diet were intragastrically treated with LPHs (or vehicle) for 12 weeks. Liver and adipose tissue lipid accumulation and hepatic inflammatory and oxidant status were evaluated. A significant decrease in steatosis was observed in LPHs-treated mice, which presented a decreased gene expression of CD36 and LDL-R, crucial markers in MAFLD. In addition, LPHs increased the hepatic total antioxidant capacity and reduced the hepatic inflammatory status. Moreover, LPHs-treated mice showed a significant reduction in abdominal adiposity. This is the first study to show that the supplementation with LPHs markedly ameliorates the generation of the steatotic liver caused by the intake of a Western diet and reduces abdominal obesity in ApoE^−/− mice. Future clinical trials should shed light on the effects of LPHs on MAFLD. Full article

Lupin protein isolate was treated using the combination of enzymatic hydrolysis (Papain, Alcalase 2.4 L and Pepsin) and lactic acid fermentation (Lactobacillus sakei ssp. carnosus, Lactobacillus amylolyticus and Lactobacillus helveticus) to investigate the effect on functional properties, sensory profile and protein integrity. The results showed increased foaming activity (2466–3481%) and solubility at pH 4.0 (19.7–36.7%) of all fermented hydrolysates compared to the untreated lupin protein isolate with 1613% of foaming activity and a solubility of 7.3 (pH 4.0). Results of the SDS-PAGE and Bead-Assay showed that the combination of enzymatic hydrolysis and fermentation of LPI was effective in reducing L. angustifolius major allergen Lup an 1 to a residual level of <0.5%. The combination of enzymatic hydrolysis and fermentation enables the production of food ingredients with good functional properties in terms of protein solubility and foam formation, with a balanced aroma and taste profile. Full article

Alzheimer’s disease (AD), which is characterized by a devastating and progressive loss of memory, is the principal neurodegenerative disease in the elderly population worldwide. As a consequence, AD patients present neuropsychiatric symptoms, such as anxiety, causing sleeping difficulty, irritability, agitation, or aggressiveness. Previous studies have demonstrated that a high-fat diet, in addition to exacerbating AD, aggravates anxiety. We have demonstrated that Lupinus angustifolius protein hydrolysates (LPHs) have anti-inflammatory and antioxidant effects, key factors for AD and anxiety. Thus, this study aimed to evaluate the potential effects of LPHs on spatial memory and anxiety of a preclinical model of AD. ApoE^−/− mice fed with a western diet were intragastrically treated with LPHs (or a vehicle) for 14 weeks. Spatial memory and anxiety were then assessed through the Morris water maze and elevated plus maze, respectively. The results did not show significant differences in spatial memory between groups. However, a significant increase (p < 0.05) in time in open arms, center time, the number of crossings, and a reduction of anxiety behavior were observed in LPH-treated mice. This is the first study showing that an LPH treatment causes anxiolytic effects, pointing to LPHs as a potential component of future nutritional therapies. Full article