Structural, material and antibacterial properties of quercetin incorporated soy protein isolate films and its binding behavior through molecular docking.

This study aimed to investigate the three different methods for the fabrication of quercetin (1%-3% w/w of protein) incorporated soy protein isolate (SPI) films and their effect on material properties. The quercetin incorporated SPI films prepared by these methods were characterized by Fourier transform infrared (FTIR) spectroscopy, UV-Vis spectrophotometer, tensile properties, and water uptake and leaching properties. The cross-linking pattern was revealed by the FTIR spectrum that showed formation of an ester group because of interaction between the quercetin hydroxyl group and the carboxyl side chain of SPI amino acids. The tensile strength of SPI films were enhanced with the addition of quercetin as it increased to a maximum of 6.17 MPa while neat SPI film had tensile strength 4.13 MPa. The prepared films exhibit significant antibacterial activity against Listeria monocytogenes and Escherichia coli. The In-silico docking analysis demonstrates that covalent and non-covalent forces play crucial roles in binding interaction. It shows the formation of four hydrogen bonds, two salt bridges along with one pi-alkyl interaction. The simulation studies reflect the crucial amino acid residues involved in SPI-quercetin binding. The effect of quercetin binding with SPI on its stability and compactness is revealed by Root mean square deviation (RMSD) and radius of gyration studies.

Fabrication of soy protein-polyphenol covalent complex nanoparticles with improved wettability to stabilize high-oil-phase curcumin emulsions.

BACKGROUND: Recent studies have shown that the wettability of protein-based emulsifiers is critical for emulsion stability. However, few studies have been conducted to investigate the effects of varying epigallocatechin gallate (EGCG) concentrations on the wettability of protein-based emulsifiers. Additionally, limited studies have examined the effectiveness of soy protein-EGCG covalent complex nanoparticles with improved wettability as emulsifiers for stabilizing high-oil-phase (≥ 30%) curcumin emulsions. RESULTS: Soy protein isolate (SPI)-EGCG complex nanoparticles (SPIEn) with improved wettability were fabricated to stabilize high-oil-phase curcumin emulsions. The results showed that EGCG forms covalent bonds with SPI, which changes its secondary structure, enhances its surface charge, and improves its wettability. Moreover, SPIEn with 2.0 g L -1 EGCG (SPIEn-2.0) exhibited a better three-phase contact angle (56.8 ± 0.3o) and zeta potential (-27 mV) than SPI. SPIEn-2.0 also facilitated the development of curcumin emulsion gels at an oil volume fraction of 0.5. Specifically, the enhanced network between droplets as a result of the packing effects and SPIEn-2.0 with inherent antioxidant function was more effective at inhibiting curcumin degradation during long-term storage and ultraviolet light exposure. CONCLUSION: The results of the present study indicate that SPIEn with 2.0 g L -1 EGCG (SPIEn-2.0) comprises the optimum conditions for fabricating emulsifiers with improved wettability. Additionally, SPIEn-0.2 can improve the physicochemical stability of high-oil-phase curcumin emulsions, suggesting a novel strategy to design and fabricate high-oil-phase emulsion for encapsulating bioactive compounds. © 2024 Society of Chemical Industry.

Fabrication and characterization of soy protein isolation-ferulic acid antioxidant hydrogels.

BACKGROUND: Soy protein gel products are prone to direct oxidation by reactive oxygen during processing and transportation, thus reducing their functional properties and nutritional values. A covalent complex was prepared with soy protein isolate (SPI) and ferulic acid (FA) catalyzed by laccase (LC). The complex was further treated with microbial transglutaminase (TGase) to form hydrogels. The structural changes of the covalent complex (SPI-FA) and the properties and antioxidant stability of hydrogel were investigated. RESULTS: The SPI-FA complexes were demonstrated to be covalently bound by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and they had the least hydrophobic and free sulfhydryl groups at a 1.0 mg mL-1 FA concentration. The α-helix of complexes increased from 11.50% to 27.39%, and random coil dropped from 26.06% to 14.44%. The addition of FA caused SPI fluorescence quenching and redshift. The hydrogel was formed after the complex was induced with TGase, and its hardness and water holding capacity was increased by 50.61% and 26.21%, respectively. Scanning electron microscopy showed that a layered and ordered gel structure was formed. After in vitro digestion, the complex hydrogels maintained stable antioxidant activity, and the free radical scavenging rates of DPPH and ABTS reached 87.65% and 84.45%, respectively. CONCLUSION: SPI-FA covalent complexes were prepared under laccase catalysis, and complex hydrogels were formed by TGase. Hydrogels have stable antioxidant activity, which provides application prospects for the antioxidant development of food. © 2023 Society of Chemical Industry.

Effects of soy protein isolate interaction with brown rice starch on the multiscale structure of brown rice bread.

BACKGROUND: Gluten-free bread (GFB) has technical bottlenecks such as hard texture, rough taste and low nutrition in practical production. In order to solve these problems, this study used germinated brown rice starch as the main raw material, and investigated the effects of soybean isolate protein (SPI) on the multiscale structure of germinated brown rice starch and bread quality. RESULTS: A gluten-free rice bread process simulation system was established, and the interaction between SPI and starch in the simulation system was characterized. The result shows that the interaction forces between SPI and germinated brown rice starch were mainly represented by hydrogen bonds, and with the addition of SPI, the crystallinity of starch showed a downward trend. At the same time, when the amount of SPI was 3%, the appearance quality was the best and the specific volume of bread was 1.08 mL g-1. When the amount of SPI was 6%, the texture quality was the best. Compared with the bread without SPI, the hardness of the bread with 6% SPI was reduced by 0.13 times, the springiness was increased by 0.03 times, the color was the most vibrant, the L* value being 1.02 times the original, and the baking loss was reduced to 0.98 times the original. CONCLUSIONS: The interaction force between SPI and germinated brown rice starch and its effect on bread quality were clarified, and these results inform choices about providing a theoretical basis for the subsequent development of higher-quality GFB. © 2024 Society of Chemical Industry.

Improved encapsulation efficiency and storage stability of lutein by soy protein isolate nanocarriers with thermal and trypsin treatments.

BACKGROUND: Encapsulation of bioactive compounds within protein-based nanoparticles has garnered considerable attention in the food and pharmaceutical industries because of its potential to enhance stability and delivery. Soy protein isolate (SPI) has emerged as a promising candidate, prompting the present study aiming to modify its properties through controlled thermal and trypsin treatments for improved encapsulation efficiency (EE) of lutein and its storage stability. RESULTS: The EE of lutein nanoparticles encapsulated using SPI trypsin hydrolysates (SPIT) with three varying degrees of hydrolysis (4.11%, 6.91% and 10.61% for SPIT1, SPIT2 and SPIT3, respectively) increased by 12.00%, 15.78% and 18.59%, respectively, compared to SPI. Additionally, the photostability of SPIT2 showed a remarkable increase of 38.21% compared to SPI. The superior encapsulation efficiency and photostability of SPIT2 was attributed to increased exposure of hydrophobic groups, excellent antioxidant activity and uniform particle stability, despite exhibiting lower binding affinity to lutein compared to SPI. Furthermore, in SPIT2, the protein structure unfolded, with minimal impact on overall secondary structure upon lutein addition. CONCLUSION: The precise application of controlled thermal and trypsin treatments to SPI has been shown to effectively produce protein nanoparticles with substantially improved encapsulation efficiency for lutein and enhanced storage stability of the encapsulated lutein. These findings underscore the potential of controlled thermal and trypsin treatments to modify protein properties effectively and offer significant opportunities for expanding the applications of protein-based formulations across diverse fields. © 2024 Society of Chemical Industry.

Tri-component hydrocolloid as egg white replacement in meringues: gellan gum with soy protein isolate and maltodextrin.

BACKGROUND: In the quest for sustainable food ingredients, the present study delves into the potential of a tri-component hydrocolloid blend, comprising gellan gum (GG), soy protein isolate (SPI) and maltodextrin (MD), as a replacement for egg white in meringue production. The research aims to elucidate the intricate physical properties of meringue containing this tri-component structure, focusing on foaming dynamics, rheological behavior and the textural properties of the resulting meringue cookies. RESULTS: Experiments were conducted with various hydrocolloids (k-carrageenan, GG, and locust bean gum) and GG was identified as optimal for improving foaming capacity and foaming stability. Rheological evaluations showed a positive correlation between increased GG concentration within the tri-component matrix and an increase in both storage modulus (G') and loss modulus (G"), indicating improved structural integrity. Furthermore, a comparative analysis of the texture profiles of cookies prepared with this blend highlighted the ability of higher GG concentrations to satisfactorily replicate the tactile and visual qualities of traditional egg white-based meringues. This result was particularly evident compared to formulations utilizing solely SPI or the combined SPI-MD configuration. CONCLUSION: Conclusively, the results of the present study highlight the significant potential of the GG-SPI-MD tri-component structure to closely mimic the critical properties of egg white, thus offering a promising plant-based alternative for meringue production. © 2024 Society of Chemical Industry.

Effect of transglutaminase crosslinking combined with lactic fermentation on the potential allergenicity and conformational structure of soy protein.

BACKGROUND: Food allergies are a growing concern worldwide, with soy proteins being important allergens that are widely used in various food products. This study investigated the potential of transglutaminase (TGase) and lactic acid bacteria (LAB) treatments to modify the allergenicity and structural properties of soy protein isolate (SPI), aiming to develop safer soy-based food products. RESULTS: Treatment with TGase, LAB or their combination significantly reduced the antibody reactivity of ß-conglycinin and the immunoglobulin E (IgE) binding capacity of soy protein, indicating a decrease in allergenicity. TGase treatment led to the formation of high-molecular-weight aggregates, suggesting protein crosslinking, while LAB treatment resulted in partial protein hydrolysis. These structural changes were confirmed by Fourier transform infrared spectroscopy, which showed a decrease in ß-sheet content and an increase in random coil and ß-turn contents. In addition, changes in intrinsic fluorescence and ultraviolet spectroscopy were also observed. The alterations in protein interaction and the reduction in free sulfhydryl groups highlighted the extensive structural modifications induced by these treatments. CONCLUSION: The synergistic application of TGase and LAB treatments effectively reduced the allergenicity of SPI through significant structural modifications. This approach not only diminished antibody reactivity of ß-conglycinin and IgE binding capacity of soy protein but also altered the protein's primary, secondary and tertiary structures, suggesting a comprehensive alteration of SPI's allergenic potential. These findings provide a promising strategy for mitigating food allergy concerns and lay the foundation for future research on food-processing techniques aimed at allergen reduction. © 2024 Society of Chemical Industry.

Red dragon fruit-soy protein isolate biofilm: UV-blocking, antioxidant & improved mechanical properties for sustainable food packaging.

In this study, an active biofilm was developed by incorporating red dragon fruit peel (RDF) extract into soy protein isolate (SPI) film matrix for sustainable food packaging. The addition of betalain-rich-RDF extract (1-7 wt%) significantly improved UV-blocking and antioxidant properties of the film compared to the control film. As wt% of RDF-extract increased, water vapor permeability, water solubility, and elongation at break decreased by 1.06 × 10-10 g m m-2 s-1 Pa-1, 34.25%, and 133.25%, respectively. On the other hand, Tensile strength increased significantly (P < 0.05) by 78.76%. FTIR results confirmed the intermolecular interaction between RDF extract and SPI through hydrogen bonding, while XRD result showed a decrease in the crystallinity degree of the film with RDF extract addition. However, no significant change in the TGA curve between extract-incorporated SPI films was observed. SEM analysis revealed that SPI B and SPI D films had a more compact and denser structure than the control film, while AFM analysis showed an increase in Ra and Rq values representing higher surface roughness of SPI D film. SPI D film also significantly (P < 0.05) decreased the weight loss and increased total soluble solids of freshly cut apples over 7-day storage period. Supplementary Information: The online version contains supplementary material available at 10.1007/s13197-024-05940-2.

Soy Protein Isolate-Chitosan Nanoparticle-Stabilized Pickering Emulsions: Stability and In Vitro Digestion for DHA.

The purpose of the study was to investigate the stability and oral delivery of DHA-encapsulated Pickering emulsions stabilized by soy protein isolate-chitosan (SPI-CS) nanoparticles (SPI-CS Pickering emulsions) under various conditions and in the simulated gastrointestinal (GIT) model. The stability of DHA was characterized by the retention rate under storage, ionic strength, and thermal conditions. The oral delivery efficiency was characterized by the retention and release rate of DHA in the GIT model and cell viability and uptake in the Caco-2 model. The results showed that the content of DHA was above 90% in various conditions. The retention rate of DHA in Pickering emulsions containing various nanoparticle concentrations (1.5 and 3.5%) decreased to 80%, while passing through the mouth to the stomach, and DHA was released 26% in 1.5% Pickering emulsions, which was faster than that of 3.5% in the small intestine. After digestion, DHA Pickering emulsions proved to be nontoxic and effectively absorbed by cells. These findings helped to develop a novel delivery system for DHA.

Characterization of the interaction between allicin and soy protein isolate and functional properties of the adducts.

BACKGROUND: Soybean meal, a by-product of the soybean oil production industry, has a high protein content but the compact globular structure of the protein from soybean meal limits its wide application in food processing. Allicin has been found to have numerous functional properties. In this study, allicin was interacted with soy protein isolate (SPI). The functional properties of the adducts were investigated. RESULTS: Binding with allicin significantly quenched the fluorescence intensity of SPI. Static quenching was the main quenching mechanism. The stability of adducts decreased with increasing temperature. The greatest extent of binding between allicin and sulfhydryl groups (SH) of SPI was obtained at an allicin/SH molar ratio of 1:2. The amino groups of SPI did not bind with allicin covalently. Soy protein isolate was modified by allicin through covalent and non-covalent interactions. Compared with SPI, the emulsifying activity index and foaming capacity of adducts with a ratio of 3:1 were improved by 39.91% and 64.29%, respectively. Soy protein isolate-allicin adducts also exhibited obvious antibacterial effects. The minimum inhibitory concentrations (MICs) of SPI-allicin adducts on Escherichia coli and Staphylococcus aureus were 200 and 160 µg mL-1 , respectively. CONCLUSION: The interaction of allicin with SPI is beneficial for the functional properties of SPI. These adducts can be used in different food formulations as emulsifiers, foamers, and transport carriers. © 2023 Society of Chemical Industry.

Effect of soy protein isolate on physical properties of quinoa dough and gluten-free bread quality characteristics.

BACKGROUND: Quinoa is a good gluten-free resource for food processing, especially bread making, and can improve and prevent the development of complications associated with celiac disease (CD). However, lack of gluten affects quinoa bread quality. Previous research showed that soy protein isolate (SPI) could improve gluten-free bread quality to some extent. Therefore, this study investigated the effects of SPI on the physical properties of quinoa dough and gluten-free bread quality characteristics. RESULTS: Results showed that, with appropriate SPI substitution, the farinograph properties of quinoa flour significantly improved (P < 0.05). The sample with 8% SPI substitution showed a better development time (DT, 3.30 ± 0.20 min), stability time (ST, 8.80 ± 0.10 min) and softening degree (SD, 8.80 ± 0.10 FU), which were close to those of wheat flour, although more water absorption (WA, 76.40 ± 2.10%) was needed than for wheat flour (66.30 ± 3.10%). The extensograph properties of quinoa flour also significantly improved after 8% SPI substitution (P < 0.05). Furthermore, SPI substitution increased G' moduli of quinoa dough and decreased tan δ to some extent, providing better rheological properties closer to those of wheat dough. SPI substitution also improved the quality and texture of quinoa bread and reduced the gap with wheat bread. When SPI substitution was 8%, the specific volume, hardness and springiness of quinoa bread were 2.29 ± 0.05 mL g-1 , 1496.47 ± 85.21 g and 0.71 ± 0.03%, respectively. CONCLUSION: These results suggested that SPI substitution would be an effective way to develop higher-quality gluten-free bread. © 2022 Society of Chemical Industry.

Hydrogen bond-driven assembly of coral-like soy protein isolate-tannic acid microcomplex for encapsulation of limonene.

BACKGROUND: The encapsulation of flavor and aroma compounds has great potential in foods, while effective preparation in the food industry is still a great challenge. Inspired by leather tanning, tannic acid (TA) was used for deep crosslinking through hydrogen bond-driven assembly on soy protein isolate for encapsulating limonene with a high loading ratio. RESULTS: The added TA changed the protein structure and formed a limonene-loaded microcomplex. The morphology of these microcomplexes changed from smooth to rough, followed by the formation of smooth nanoparticle aggregates, by changing the amount of TA. The encapsulation efficiency and loading ratio were increased from 0.78% and 4.30% to 59.32% and 45.78% after increasing TA from 1.875 to 60 mg mL-1 . The result of confocal laser scanning microscopy indicated that limonene is evenly distributed in microcomplexes. Additionally, the results of thermal stability demonstrated protection of limonene by soy protein-tannic acid microcomplex. CONCLUSION: It is suggested that the added TA improved the encapsulation efficiency and loading ratio. Limonene is loaded in the complex in two ways. The present research provides a new and easy path for the preparation of the non-thermal soy protein aroma carrier. © 2022 Society of Chemical Industry.

Soy proteins as vehicles for enhanced bioaccessibility and cholesterol-lowering activity of phytosterols.

BACKGROUND: The formulation of phytosterol (PS)-enriched functional foods has attracted increasing interest in the recent years, owing to its potential health effects. However, the poor solubility and bioavailability greatly limit PS application in this regard. This study investigated whether soy protein isolate (SPI) could effectively perform as a nanocarrier for improving the water solubility, bioaccessibility, and cholesterol-lowering activity of PSs. RESULTS: In this work, we fabricated SPI-PS nanocomplexes, which not only can enhance the stability and bioaccessibility of PS, but also improve the cholesterol-lowering ability of SPI. This improvement was mainly due to the formation of protein-active substance complexes, through hydrophobic interactions. The complexation with PSs resulted in formation of nanosized particles with greater sizes, lower ζ-potential, and higher surface hydrophobicity. The encapsulation efficiency, loading amount, and solubility of PS were closely related to the applied PS concentration in the mixed dispersions, and the maximal PS solubility in the aqueous phase reached about 1.63 mg mL-1 at the highest PS concentration (2.0 mg mL-1 ). The PS molecules in the nanocomplexes were mainly present in the amorphous form. The enhanced in vitro cholesterol-lowering activity of PS nanocomplexes relative to free PS seemed to be closely related to its higher bioaccessibility. CONCLUSION: The findings are of relevance for the development of food-grade PS ingredients suitable for the formulations of PS-enriched functional foods. © 2022 Society of Chemical Industry.

Gel properties of okara dietary fiber-fortified soy protein isolate gel with/without NaCl.

BACKGROUND: Soy protein isolate (SPI) is widely used as an alternative to animal-based protein, and its gelling property is essential for producing plant protein-based foods. Insoluble dietary fiber has been used to improve the properties of protein gels. RESULTS: Effects of partial replacement of SPI by okara dietary fiber (ODF) on the gelling properties of ODF-fortified SPI gels with and without 0.1 m NaCl were investigated. The presence of ODF hindered the SPI self-aggregation and reduced the surface hydrophobicity of SPI. The presence of ODF reduced the hydrophobic interaction and improved the proportion of disulfide bonds in the gels. In the microstructure, the swollen ODF promoted the local aggregation of SPI at 0.1 m NaCl. Texture profile analysis showed that 5% and 10% ODF improved the SPI gel hardness in the absence of NaCl, whereas only 5% ODF improved the gel hardness at 0.1 m NaCl. The results of low-field nuclear magnetic resonance imaging revealed that ODF shortened the T2 relaxation time of the free water in the gel. The gel of ODF-10 had the highest storage modulus. CONCLUSION: Using an appropriate amount of ODF to replace SPI could improve the quality of SPI gel and increase the dietary fiber content in the product. In addition, the appropriate ratio of ODF/SPI varied in different solution environments. © 2022 Society of Chemical Industry.

Characterization of structural and functional properties of soy protein isolate and sodium alginate interpenetrating polymer network hydrogels.

BACKGROUND: This study used enzymatic and Ca2+ cross-linking methods to prepare edible soy protein isolate (SPI) and sodium alginate (SA) interpenetrating polymer network hydrogels to overcome the disadvantages of traditional interpenetrating polymer network (IPN) hydrogels, such as poor performance, high toxicity, and inedibility. The influence of changes in SPI and SA mass ratio on the performance of SPI-SA IPN hydrogels was investigated. RESULTS: Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM) were used to characterize the structure of the hydrogels. Texture profile analysis (TPA), rheological properties, swelling rate, and Cell Counting Kit-8 (CCK-8) were used to evaluate physical and chemical properties and safety. The results showed that, compared with SPI hydrogel, IPN hydrogels had better gel properties and structural stability. As the mass ratio of SPI-SA IPN changed from 1:0.2 to 1:1, the gel network structure of hydrogels also tended to be dense and uniform. The water retention and mechanical properties of these hydrogels, such as storage modulus (G'), loss modulus (G"), and gel hardness increased significantly and were greater than those of the SPI hydrogel. Cytotoxicity tests were also performed. The biocompatibility of these hydrogels was good. CONCLUSIONS: This study proposes a new method to prepare food-grade IPN hydrogels with mechanical properties of SPI and SA, which may have strong potential for the development of new foods. © 2023 Society of Chemical Industry.

Physicochemical and functional property of the Maillard reaction products of soy protein isolate with L-arabinose/D-galactose.

BACKGROUND: Soy protein isolate (SPI) is widely used in the food industry because of its nutritional and functional properties. During food processing and storage, the interaction with co-existing sugars can cause changes in the structural and functional properties of SPI. In this study, SPI-l-arabinose conjugate (SPI:Ara) and SPI-d-galactose conjugate (SPI:Gal) were prepared using Maillard reaction (MR), and the effects of five-carbon/six-carbon sugars on the structural information and function of SPI were compared. RESULTS: MR unfolded and stretched the SPI, changing its ordered conformation into disorder. Lysine and arginine of SPI were bonded with the carbonyl group of sugar. The MR between SPI and l-arabinose has a higher degree of glycosylation compared to d-galactose. MR of SPI enhanced its solubility, emulsifying property and foaming property. Compared with SPI:Ara, SPI:Gal exhibited better aforementioned properties. The functionalities of amphiphilic SPI were enhanced by MR, SPI:Gal possessed better hypoglycemic effect, fat binding capacity and bile acid binding ability than SPI:Ara. MR endowed SPI with enhanced biological activities, SPI:Ara showed higher antioxidant activities, and SPI:Gal exhibited stronger antibacterial activities. CONCLUSION: Our work revealed that l-arabinose/d-galactose exhibited different effects on the structural information of SPI, and further affected its physicochemical and functional property. © 2023 Society of Chemical Industry.

Preparation of high complex concentration emulsion stabilized by soy protein/dextran sulfate composite particles.

BACKGROUND: Soy protein isolate (SPI) can be used as an emulsifier to stabilize emulsions, though SPI is unstable under low acidic conditions. Stable composite particles of SPI and dextran sulfate (DS) can be formed by the electrostatic interaction at the pH 3.5. Furthermore, the SPI/DS composite particles can be used to prepare a high complex concentration emulsion. The stabilization properties of the high complex concentration emulsion were investigated. RESULTS: Compared to uncompounded SPI, the particle size of SPI/DS composite particles was smaller at 1.52 µm, and the absolute value of the potential increased to 19.9 mV when the mass ratio of SPI to DS was 1:1 and the pH was 3.5. With the DS ratio increased, the solubility of the composite particles increased to 14.44 times of the untreated protein at pH 3.5, while the surface hydrophobicity decreased. Electrostatic interactions and hydrogen bonds were the main forces between SPI and DS, and DS was electrostatically adsorbed on the surface of SPI. The emulsion stability significantly enhanced with the increase of complex concentration (38.88 times higher than at 1% concentration), the emulsion average droplet size was the lowest (9.64 µm), and the absolute value of potential was the highest (46.67 mV) when the mass ratio of SPI to DS was 1:1 and the complex concentration of 8%. The stability of the emulsion against freezing was improved. CONCLUSION: The SPI/DS complex has high solubility and stability under low acidic conditions, and the emulsion of the SPI/DS complex has good stability. © 2023 Society of Chemical Industry.

Edible, strong, and low-hygroscopic bacterial cellulose derived from biosynthesis and physical modification for food packaging.

BACKGROUND: The pervasive presence of plastic packaging has led to significant environmental contamination due to excessive reliance on petrochemicals and the inherent non-biodegradability of these materials. Bacterial cellulose (BC) films present a viable alternative for food packaging applications, owing to their environmentally friendly synthesis process, non-toxic nature, robust mechanical strength, and biodegradability. However, the high hygroscopicity of such bio-based materials has limited their widespread adoption, as it results in diminished strength and barrier properties. In this study, a novel approach for creating edible, transparent, robust, and high-barrier BC-based composite packaging was proposed through biosynthesis with the incorporation of soy protein isolate and the physical interpenetration of calcium alginate-polyethylene glycol as a composite coating. RESULTS: The finding demonstrated that the synthesized bio-based composite material exhibits stability in water, high optical transparency, complete oil resistance, and full degradability within 1 to 2 months. Furthermore, the composite material displayed enhanced mechanical properties in both dry and wet conditions, with a tensile strength of approximately 84 MPa, outperforming commercially available kraft paper and low-density polyethylene. CONCLUSIONS: Soy protein isolate established a rigid, coherent, and homogeneous network with BC fibrils, thereby augmenting mechanical properties. Calcium alginate can be effectively combined with BC, utilizing polyethylene glycol as a binder and plasticizer, to generate a densely packed structure with reduced hygroscopicity. This bio-based composite material demonstrated considerable potential for application in food packaging and other value-added sectors as a substitute for non-degradable plastics. © 2023 Society of Chemical Industry.

Application of soy protein isolate-xylose conjugates for improving the viability and stability of probiotics microencapsulated by spray drying.

BACKGROUND: Production and consumption of probiotics need to meet many adverse stresses, which can reduce their health-promoting effects on humans. Microencapsulation is an effective technique to improve the biological activity of probiotics and wall materials are also required during encapsulation. Application of Maillard reaction products (MRPs) in probiotic delivery is increasing. RESULTS: This work aims to study the effects of soy protein isolate (SPI)-xylose conjugates heated at different times on the viability and stability of probiotics. SPI-xylose MRPs formed after heat treatment based on changes in the browning intensity, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Fourier transform infrared spectroscopy. After heat treatment, α-helix and ß-sheet contents of SPI-xylose mixture shifted from 11.3% and 31.3% to 6.4-11.0% and 31.0-36.9%, respectively, and the thermal stability slightly changed. During spray drying, except for MRP240@LAB, probiotic viability was higher in the MRP-based probiotic microcapsules (21.36-25.31%) than in Mix0@LAB (20.17%). MRP-based probiotic microcapsules had smaller particle sizes (431.1-1243.0 nm vs. 7165.0 nm) and greater intestinal digestion tolerance than Mix0@LAB. Moreover, the MRP-based probiotic microcapsules showed better storability than Mix0@LAB and adequate growth and metabolism capacity. CONCLUSION: SPI-xylose Maillard reaction products are a promising wall material for probiotics microencapsulation, which can improve bacterial survivability during spray drying and enhance bacterial gastrointestinal digestion resistance. This study sheds light on preparing probiotic microcapsules with superior properties by spray drying. © 2023 Society of Chemical Industry.

Optimization of enzymatic soy protein isolate-glucosamine conjugates to improve the freeze-thaw stability of emulsion.

BACKGROUND: Using transglutaminase (TGase) is a new method to improve protein properties in order to promote protein glycosylation. This article mainly studies soy protein isolate (SPI) and glucosamine to improve the freeze-thaw stability of emulsion under the action of TGase. The degree of glycosylation was studied by the content of free amino groups and the degree of conjugation. The optimal conditions for preparing soy protein isolate-glucosamine (SPI-G) conjugate were determined by a response surface optimization model based on single-factor experiments using the creaming index of the emulsion after the first freeze-thaw cycle as the response value. RESULTS: The results showed that the emulsion had the lowest creaming index when the conditions of protein concentration was 20 g L-1 , mass ratio of SPI-G was 5:3 (w/w), enzyme addition amount was 10 U g-1 , and reaction time was 2 h. The optimized modified product was measured for the creaming index after the first freeze-thaw cycle. It was found that the creaming index of the modified product SPI-G after the first freeze-thaw cycle was 9.02%, which was less than and close to the optimized model predicted value. The creaming index and optical microscopy results after three freeze-thaw cycles confirmed that the freeze-thaw stability of the SPI-G samples was significantly enhanced after optimization of the response surface model. CONCLUSION: It showed that glycosylation promoted by TGase could improve the freeze-thaw stability of SPI emulsion, thereby broadening the application of SPI in food. © 2022 Society of Chemical Industry.