Search Results (53)

Consumer demand for dairy products like cheese and curds has resulted in a rise in whey production, which has caused significant waste and environmental issues. For this reason, improving the functional characteristics of whey proteins and their usage value are essential. In this study, camel whey protein–galactose conjugates (CWP-Gal) and camel whey protein–glucose conjugates (CWP-Glu) were prepared through the Maillard reaction, and their structural and functional properties were characterized. Improvements in solubility of 14.90% and 8.17%, emulsification activity of 15.53% and 13.64%, and foaming capacity of 113.95% and 106.03% were demonstrated by CWP-Gal and CWP-Glu in comparison to camel whey protein (CWP). Circular dichroism analysis revealed secondary structure alterations in CWP-Gal and CWP-Glu compared to CWP. SDS-PAGE, FT-IR, and intrinsic fluorescence spectroscopy all verified that sugar molecules and proteins were covalently conjugated. SEM analysis revealed that the conjugates had a more sparsely packed microstructure. The results demonstrate that CWP-Gal exhibits enhanced structural stability and superior functional properties, providing a scientific basis for its potential utilization in the food industry. Full article

The covalent interactions of polysaccharides and protein can improve the emulsification and stability of Pickering emulsions, which are promising systems for the delivery of active substances. Okra flowers, which commonly represent agricultural waste, have high-viscosity polysaccharides that can be used for the development of protein–polysaccharide-based emulsifiers. In this study, the Maillard reaction was performed under optimized conditions (70 °C, pH 10, and 12 h) with a 1:1 mass ratio to generate pea protein isolate (PPI)–okra flower polysaccharide (OP) conjugate with the highest grafting degree of 22.80 ± 0.26%. The covalent binding of OP facilitated variations in the secondary and tertiary structures of PPI, decreasing its particle size (from 535.70 to 212.05 nm) and zeta-potential (from −30.37 to −44.39 mV). The emulsifying stability of the emulsion stabilized by OP-PPI conjugates was significantly improved due to the formation of a stable interfacial layer, showing an 80.39% increase compared to that of free PPI. Simultaneously, the emulsions prepared with the conjugates demonstrated excellent stability across diverse environmental conditions by enhancing the interaction between the lipid and protein. Moreover, the conjugate-stabilized emulsion not only exhibited a higher encapsulation efficiency of 91.52 ± 0.75% and superior protective efficacy but also controlled the release of apigenin (API) during gastrointestinal digestion, achieving the highest API bioaccessibility (74.58 ± 1.19%). Furthermore, it also contributed to the absorption and transmembrane transport efficiency of API in Caco-2 cells, improving its bioavailability. These results confirmed that covalent conjugation with OP is a valuable strategy for enhancing the emulsifying features of PPI. The PPI–OP emulsion delivery system holds great potential for nutrient delivery. Full article

Protein conjugation with the Maillard reaction has received considerable attention in the past decades in terms of improving functional properties. This study evaluated the changes in the techno-functional properties of whey protein isolate (WPI), soy protein isolate (SPI), and albumin (Alb) after conjugation with basil seed gum (BSG). The conjugates were developed via the Maillard reaction. Various analyses including FT-IR, XRD, SEM, SDS-PAGE, DSC, RVA, rheology, zeta potential, emulsion, and foaming ability were used for evaluating conjugation products. Conjugation between proteins (WPI, SPI, Alb) and BSG was validated by FT-IR spectroscopy. XRD results revealed a decrease in the peak of BSG after conjugation with proteins. SDS-PAGE demonstrated the conjugation of WPI, SPI, and Alb with BSG. DSC results showed that conjugation with BSG reduced the T_g of WPI, SPI, and Alb from 210.21, 207.21, and 210.90 °C to 190.30, 192.91, and 196.66 °C, respectively. The emulsion activity and emulsion stability of protein/BSG conjugates were increased significantly. The droplet size of emulsion samples ranged from 112.1 to 239.3 nm on day 3. Nanoemulsions stabilized by Alb/BSG conjugate had the smallest droplet sizes (112.1 and 143.3 nm after 3 and 17 days, respectively). The foaming capacity of WPI (78.57%), SPI (61.91%), and Alb (71.43%) in their mixtures with BSG increased to 107.14%, 85.71%, and 85.71%, respectively, after making conjugates with BSG. The foam stability of WPI (39.34%), SPI (61.57%), and Alb (53.37%) in their mixtures with BSG (non-conjugated condition) increased to 77.86%, 77.91%, and 72.32%, respectively, after formation of conjugates with BSG. Conjugation of BSG to proteins can improve the BSG applications as a multifunctional stabilizer in pharmaceutical and food industries. Full article

This study investigated the physicochemical and emulsifying properties of chickpea protein isolate (CPI)-citrus pectin (CP) conjugates formed via the Maillard reaction across varying reaction durations. CPI and CP were conjugated under controlled dry-heating conditions, and the resulting conjugates were characterized by measuring their particle size, zeta potential, solubility, thermal stability, surface hydrophobicity, and emulsifying properties. The results showed that as reaction duration increased, the particle size and zeta potential of the CPI-CP conjugates increased significantly, reaching a maximum particle size of 1311.33 nm and a zeta potential of −35.67 mV at 12 h. Moreover, the Maillard reaction improved the solubility, thermal stability, and hydrophobicity of the CPI. Glycosylation increased the emulsifying activity index (EAI) and emulsifying stability index (ESI) of the CPI to 145.33 m²/g and 174.51 min, respectively. Optimal emulsions were achieved at a protein concentration of 1.5 wt% and a 10% volume fraction of the oil phase. The Maillard reaction promoted the interfacial protein content and the thickness of the interfacial layer while decreasing the droplet size and zeta potential of the emulsion. Additionally, the emulsion prepared with CPI-CP-12 h showed outstanding long-term stability. These results demonstrate that a moderate Maillard reaction with CP effectively enhances the physicochemical and emulsifying characteristics of CPI. Full article

Emulsions are widely utilized in food systems but often face stability challenges due to environmental stresses, such as pH, ionic strength, and temperature fluctuations. Fish skin gelatin (FSG), a promising natural emulsifier, suffers from limited functional properties, restricting its broader application. This study explored the enhancement of emulsion stability in Litsea cubeba essential oil systems through the glycosylation of fish skin gelatin (FSG) with dextran via the dry Maillard reaction. Among dextrans of varying molecular weights (10 kDa, 100 kDa, 200 kDa, and 500 kDa), the 200 kDa dextran exhibited the best emulsification performance, achieving a remarkable 160.49% increase in stability index. The degree of grafting (DG) increased with molecular weight, peaking at 34.77% for the 500 kDa dextran, followed by 23.70% for the 200 kDa variant. The particle size of the FSG–Dex 200 kDa conjugate emulsion was reduced to 639.1 nm, compared to 1009–1146 nm for the unmodified FSG, while hydrophobicity improved by 100.56%. The zeta potential values approached 30 mV, indicating enhanced stability. Furthermore, glycosylation significantly improved antioxidant activity, as evidenced by increased radical scavenging capacity in both DPPH and ABTS assays. These findings underscore the potential of glycosylated FSG as a natural emulsifier in food applications. Full article

This study explored the structural features and foaming properties of ovalbumin (OVA) and its glycosylated conjugates with citrus pectin (CP) formed through the Maillard reaction. The results demonstrated that OVA and CP were successfully conjugated, with the degree of grafting increasing to 43.83% by day 5 of the reaction. SDS-PAGE analysis confirmed the formation of high-molecular-weight conjugates. Fourier-transform infrared (FT-IR) and fluorescence spectroscopy further revealed alterations in the secondary and tertiary structures of OVA, including an enhanced β-sheet content, a reduced β-turn content, and the depletion of tryptophan residues. Moreover, the surface hydrophobicity of the OVA–CP conjugates significantly increased, enhancing foaming properties. Furthermore, the analysis of foaming properties exhibited that the Maillard reaction improved the foaming capacity of OVA to 66.22% and foaming stability to 81.49%. These findings highlight the potential of glycosylation via the Maillard reaction to significantly improve the foaming properties of OVA, positioning it as a promising novel foaming agent. Full article

The non-enzymatic conjugation of peptides through the Maillard reaction has gained attention as an effective method to enhance biological functions. This study focuses on two conjugate mixtures: crude soy protein hydrolysate (SPH) conjugated with mannose (SPHM) and crude soy protein hydrolysate conjugated with allulose (SPHA). These two mixtures were products of the Maillard reaction, also known as non-enzymatic glycation. In vitro experiments were conducted to evaluate the antioxidant, anti-pancreatic lipase, inhibition of Bovine Serum Albumin (BSA) denaturation, and anti-angiotensin converting enzyme (ACE) activities of these conjugated mixtures. The results indicate that conjugated mixtures significantly enhance the antioxidant potential demonstrated via the DPPH and FRAP assays. SPHA exhibits superior DPPH scavenging activity (280.87 ± 16.39 µg Trolox/mL) and FRAP value (38.91 ± 0.02 mg Trolox/mL). Additionally, both conjugate mixtures, at a concentration of 10 mg/mL, enhance the BSA denaturation properties, with SPHM showing slightly higher effectiveness compared to SPHA (19.78 ± 2.26% and 5.95 ± 3.89%, respectively). SPHA also shows an improvement in pancreatic lipase inhibition (29.43 ± 1.94%) when compared to the SPHM (23.34 ± 3.75%). Furthermore, both the conjugated mixtures and rare sugars exhibit ACE inhibitory properties on their own, effectively reducing ACE activity. Notably, the ACE inhibitory effects of the individual compounds and their conjugate mixtures (SPHM and SPHA) are comparable to those of positive control (Enalapril). In conclusion, SPHM and SPHA demonstrate a variety of bioactive properties, suggesting their potential use in functional foods or as ingredients in supplementary products. Full article

This study addresses the growing interest in natural functional ingredients by evaluating the prebiotic and health-promoting functions of honeybee brood biopeptides (HBb-Bps) and their conjugates. The purpose was to investigate their antioxidant activities, enzyme inhibition properties, and effects on probiotic growth and short-chain fatty acid (SCFA) production. The HBb-Bps were conjugated with honey, glucose, and fructose via the Maillard reaction. Antioxidant activities were assessed using DPPH and ABTS assays. The inhibitory effects on amylase, pancreatic lipase, and the angiotensin-converting enzyme (ACE) were measured. Probiotic growth and SCFA production were evaluated using L. plantarum TISTR846, and L. lactis TISTR1464. The HBb-Bps and their conjugates exhibited enhanced antioxidant activities post-Maillard reaction. They showed moderate enzyme inhibition, which decreased after conjugation. However, ACE inhibition increased with conjugation. The HBb-Bps significantly promoted probiotic growth and SCFA production, with further enhancement by the Maillard reaction. Overall, the HBb-Bps and their conjugates demonstrate significant prebiotic and health-promoting functions, suggesting their potential as natural ingredients in functional foods and nutraceuticals. Further research should focus on the in vivo effects and, given their solubility and stability these biopeptides could be incorporated into functional food formulations, such as health beverages, protein bars, and other fortified foods designed to deliver specific health benefits. Full article

As a protein extracted from soybeans, soy protein isolate (SPI) may undergo the Maillard reaction (MR) with co-existing saccharides during the processing of soy-containing foods, potentially altering its structural and functional properties. This work aimed to investigate the effect of mono- and polysaccharides on the structure and functional properties of SPI during MR. The study found that compared to oat β-glucan, the reaction rate between SPI and D-galactose was faster, leading to a higher degree of glycosylation in the SPI–galactose conjugate. D-galactose and oat β-glucan showed different influences on the secondary structure of SPI and the microenvironment of its hydrophobic amino acids. These structural variations subsequently impact a variety of the properties of the SPI conjugates. The SPI–galactose conjugate exhibited superior solubility, surface hydrophobicity, and viscosity. Meanwhile, the SPI–galactose conjugate possessed better emulsifying stability, capability to produce foam, and stability of foam than the SPI–β-glucan conjugate. Interestingly, the SPI–β-glucan conjugate, despite its lower viscosity, showed stronger hypoglycemic activity, potentially due to the inherent activity of oat β-glucan. The SPI–galactose conjugate exhibited superior antioxidant properties due to its higher content of hydroxyl groups on its molecules. These results showed that the type of saccharides had significant influences on the SPI during MR. Full article

β C-S lyases (β-CSLs; EC 4.4.1.8) are enzymes catalyzing the dissociation of β carbon–sulfur bonds of cysteine S-conjugates to produce odorant metabolites with a free thiol group. These enzymes are increasingly studied for their role in flavor generation in a variety of food products, whether these processes occur directly in plants, by microbial β-CSLs during fermentation, or in the mouth under the action of the oral microbiota. Microbial β-CSLs react with sulfur aroma precursors present in beverages, vegetables, fruits, or aromatic herbs like hop but also potentially with some precursors formed through Maillard reactions in cooked foods such as meat or coffee. β-CSLs from microorganisms like yeasts and lactic acid bacteria have been studied for their role in the release of polyfunctional thiols in wine and beer during fermentation. In addition, β-CSLs from microorganisms of the human oral cavity were shown to metabolize similar precursors and to produce aroma in the mouth with an impact on retro-olfaction. This review summarizes the current knowledge on β-CSLs involved in flavor generation with a focus on enzymes from microbial species present either in the fermentative processes or in the oral cavity. This paper highlights the importance of this enzyme family in the food continuum, from production to consumption, and offers new perspectives concerning the utilization of β-CSLs as a flavor enhancer. Full article

Multiple emulsions can dissolve some substances with different properties, such as hydrophilicity and lipophilicity, into different phases. They play an important role in protection, controlled release and targeted release of the encapsulated substances. However, it’s poor stability has always been one of the main problems restricting its application in the food industry. For this reason, a heat-induced aggregate (HIA) of Maillard graft product of isomalto-oligosaccharides (IMO), as well as egg white protein (EWP), was used as hydrophilic emulsifier to improve the stability of W₁/O/W₂ emulsions. Moreover, gelatin was added into the internal aqueous phase (W₁) to construct W₁/O/W₂ emulsion-gels system. The encapsulation efficiency of HIA-stabilized W₁/O/W₂ emulsions remained nearly unaltered, dropping by only 0.86%, significantly outperforming the conjugates and physical mixture of IMO and EWP in terms of encapsulation stability. The emulsion-gels system was constructed by adding 5% gelatin in the W₁, and had the highest EE% and good salt and heat stability after 30 days of storage. This experiment provides guidance for improving the stability of W₁/O/W₂ emulsions system and its application in the package delivery of functional substances in the food field. Full article

Valorisation of food by-products, like spent brewer’s yeast and fruit pomaces, represents an important strategy for contributing to sustainable food production. The aims of this study were to obtain Maillard conjugates based on spent yeast protein hydrolysate (SYH) with dextran (D) or maltodextrin (MD) by means of ultrasound treatment and to use them for developing encapsulation systems for the anthocyanins from aronia pomace. The ultrasound-assisted Maillard conjugation promoted the increase of antioxidant activity by about 50% compared to conventional heating and SYH, and was not dependent on the polysaccharide type. The ability of the conjugates to act as wall material for encapsulating various biologically active compounds was tested via a freeze-drying method. The retention efficiency ranged between 58.25 ± 0.38%–65.25 ± 2.21%, while encapsulation efficiency varied from 67.09 ± 2.26% to 88.72 ± 0.33%, indicating the strong effect of the carrier material used for encapsulation. The addition of the hydrolysed yeast cell wall played a positive effect on the encapsulation efficiency of anthocyanins when used in combination with the SYH:MD conjugates. On the other hand, the stability of anthocyanins during storage, as well as their bioavailability during gastrointestinal digestion, were higher when using the SYH:D conjugate. The study showed that hydrolysis combined with the ultrasound-assisted Maillard reaction has a great potential for the valorisation of spent brewer’s yeast as delivery material for the encapsulation of bioactive compounds. Full article

A reliable strategy for improving the stability and shelf life of protein-stabilized systems is by covalently attaching the protein onto a polysaccharide. In this study, ovalbumin (OVA) was modified with dextran (DEX) of different molecular weights by the Maillard reaction, and was used to enhance the stability of emulsions loaded with resveratrol. The surface hydrophobicity, thermal stability, and FT-IR spectroscopy of the OVA–DEX conjugates were evaluated. The results showed that the surface hydrophobicity of OVA decreased, while the thermal stability of OVA was significantly improved after DEX covalent modification. The OVA–DEX1k-stabilized emulsion exhibited high encapsulation efficiency of resveratrol, with the value of 89.0%. In addition, OVA–DEX was considerably more effective in droplet stabilization against different environmental stresses (heat, pH, and ionic strength). After 28 days of storage at 25 °C, the OVA-stabilized emulsion showed faster decomposition of resveratrol, whereas the OVA–DEX-conjugate-stabilized emulsion had approximately 73% retention of resveratrol. Moreover, the antioxidant activity of resveratrol-loaded emulsions stabilized by OVA–DEX was higher during storage under different temperatures. These results proved that the OVA–DEX conjugates had the potential to form stable, food-grade emulsion-based delivery systems against environmental stresses, which strongly supports their potential in the field of food and biomedical applications. Full article

Conjugation with glucose (G) and fructose (F) via the Maillard reaction under the wet-heating condition is a natural and non-toxic method of improving the technological functions of 7S/11S proteins in different kinds of gels. It may be used as an affordable supply of emulsifiers and an excellent encapsulating matrix for gels. This study aimed to create a glucose/fructose-conjugated 7S/11S soy protein via the Maillard reaction. The conjugation was confirmed by determining the SDS-PAGE profile and circular dichroism spectra. In addition, these conjugates were comprehensively characterized in terms of grafting degree, browning degree, sulfhydryl content, surface hydrophobicity (H₀), and differential scanning calorimetry (DSC) through various reaction times (0, 24, 48, and 72 h) to evaluate their ability to be used in food gels. The functional characteristics of the 7S/11S isolate–G/F conjugate formed at 70 °C, with a high degree of glycosylation and browning, were superior to those obtained at other reaction times. The SDS-PAGE profile indicated that the conjugation between the 7S and 11S proteins and carbohydrate sources of G and F through the Maillard reaction occurred. Secondary structural results revealed that covalent interactions with G and F affected the secondary structural components of 7S/11S proteins, leading to increased random coils. When exposed to moist heating conditions, G and F have significant potential for protein alteration through the Maillard reaction. The results of this study may provide new insights into protein modification and establish the theoretical basis for the therapeutic application of both G and F conjugation with soy proteins in different food matrixes and gels. Full article

This study investigated the formation of soy protein isolate hydrolysate–yeast cell extract (SPIH-YCE) conjugates through a humid–dry heating process and their impact on bioactivity. The incubation of SPIH-YCE samples at 60 °C and ~75% humidity for varying durations (0, 5, 10, 15, and 20 days) resulted in a significant decrease in reducing sugars and free amino acids, while the degree of glycation increased by approximately 65.72% after 10 days. SDS-PAGE analysis and size exclusion chromatography revealed the presence of peptides and glycoprotein molecules, with an increase in the distribution of larger peptide size chains. The conjugated SPIH-YCE (10 days) exhibited the highest antioxidant capacity compared to the other samples at different incubation times. A comparative study between SPIH-YCE (day 0) and SPIH-YCE after 10 days of incubation showed significantly higher anti-inflammatory and ACE inhibitory activities for the conjugates subjected to the humid–dry heating process. This suggests that SPIH-YCE conjugates could serve as an alternative substance with the potential to provide health benefits by mitigating or preventing non-communicable diseases (NCDs). This research highlights the importance of the Maillard reaction in enhancing bioactivity and offers insights into the alterations of the chemical structure of these conjugates. Full article