Crosslinking of gelatin Schiff base hydrogels with different structural dialdehyde polysaccharides as novel crosslinkers: Characterization and performance comparison.

Few studies have been conducted on the relationship between the crosslinking ability of dialdehyde polysaccharides (DPs) with different structures and the structure and properties of hydrogels. Herein, the effects of dialdehyde sodium alginate (DSA), dialdehyde guar gum (DGG), and dialdehyde dextran (DDE) as crosslinking agents for gelatin (GE)-based hydrogels were comparatively studied. First, the structure and aldehyde content of DPs were evaluated. Subsequently, the structure, crosslinking degree, and physicochemical properties of GE/DP hydrogels were characterized. Compared with pure GE hydrogels, GE/DP hydrogels had higher thermal stability and mechanical properties. Moreover, the aldehyde content of DPs was ordered as follows: DSA < DGG < DDE. The higher crosslinking degree of the hydrogels formed by DPs with a higher aldehyde content resulted in smaller hydrogel pores, higher mechanical strength, and a lower equilibrium swelling rate. These observations provide a theoretical basis for selecting crosslinking candidates for hydrogel-specific applications.

Ultrasound-assisted modification of soybean protein isolate with L-histidine: Relationship between structure and function.

Herein, the effects of ultrasound-assisted L-histidine (L-His) on the physicochemical properties and conformation of soybean protein isolate (SPI) were investigated. Particle size, zeta potential, turbidity, and solubility were used to evaluate protein aggregation, and the relationship between structural and functional changes of the proteins was characterized using spectral analysis, surface hydrophobicity, emulsification, and antioxidant properties. After ultrasound-assisted L-His treatment, SPI exhibited a smaller particle size, higher solubility, and more homogeneous micromorphology owing to the decrease in alpha-helix content and subsequent increases in zeta potential and active sulfhydryl content. In addition, spectral analysis showed that L-His and SPI could form a complex, which changed the microenvironment of the amino acid residues in SPI, thus improving its emulsification and antioxidant properties. At the concentration of L-His was 0.3 % w/w, the nanocomplex had a smaller particle size (140.03 nm), higher ζ-potential (-23.63 mV), and higher emulsification stability (22.48 min).

Fibrillation of soy protein isolate in the presence of metal ions: Structure and gelation behavior.

The structure and functional properties of protein fibrils are closely related to environmental factors in fibrillation. Herein, soy protein isolate fibrils (SPIFs, 22 mg/mL) were prepared under acid-heating conditions in the presence of 100 mM metal ions (K+, Na+, Ca2+, Mg2+, and Fe3+). Except for Fe3+, fibrillation and subsequent larger fibril aggregates were promoted, ultimately leading to gel formation. Compared with K+ or Na+, the addition of Ca2+ or Mg2+ resulted in more organized SPIF structures with increased ß-sheet contents and higher ThT fluorescence intensities. Furthermore, both of them resulted in longer fibrils with an average contour length of 700-800 nm, which significantly enhanced the storage modulus. However, the presence of Fe3+ accelerated protein hydrolysis and inhibited SPIF formation, resulting in samples consistently exhibited liquid behavior. These findings provide a foundation for understanding the influence of metal ions on regulating the fibrillation and gelling properties of SPIFs.

Unveiling the applications of membrane proteins from oil bodies: leading the way in artificial oil body technology and other biotechnological advancements.

Oil bodies (OBs) function as organelles that store lipids in plant seeds. An oil body (OB) is encased by a membrane composed of proteins (e.g., oleosins, caleosins, and steroleosins) and a phospholipid monolayer. The distinctive protein-phospholipid membrane architecture of OBs imparts exceptional stability even in extreme environments, thereby sparking increasing interest in their structure and properties. However, a comprehensive understanding of the structure-activity relationships determining the stability and properties of oil bodies requires a more profound exploration of the associated membrane proteins, an aspect that remains relatively unexplored. In this review, we aim to summarize and discuss the structural attributes, biological functions, and properties of OB membrane proteins. From a commercial perspective, an in-depth understanding of the structural and functional properties of OBs is important for the expansion of their applications by producing artificial oil bodies (AOB). Besides exploring their structural intricacies, we describe various methods that are used for purifying and isolating OB membrane proteins. These insights may provide a foundational framework for the practical utilization of OB membrane proteins in diverse applications within the realm of AOB technology, including biological and probiotic delivery, protein purification, enzyme immobilization, astringency detection, and antibody production.

Comparison of the physical stability, microstructure and protein-lipid co-oxidation of O/W emulsions stabilized by l-arginine/l-lysine-modified soy protein hydrolysate.

This work investigated the physical stability, microstructure, and oxidative stability of the emulsions prepared by soy protein hydrolysate (SPH) after modification with different concentrations of l-arginine and l-lysine. l-Arginine and l-lysine significantly increased the absolute zeta potential values, and decreased droplet sizes of the emulsions, thereby improving the physical stability of the emulsions. Meanwhile, l-arginine and l-lysine markedly decreased the apparent viscosity of the emulsions. The measurement of interfacial protein adsorption percentage showed that l-arginine (≤0.5 %) promoted the adsorption of SPH at the oil-water interface, whereas l-lysine (≤1%) reduced the adsorption of SPH at the oil-water interface. In addition, l-arginine and l-lysine (≤0.5 %) could retard lipid and protein oxidation. Correlation analysis indicated that the improvement in the physical stability of the emulsions by l-arginine and l-lysine also enhanced the oxidative stability of the emulsions. In summary, l-arginine and l-lysine could be effective modifiers for the protein-based emulsion systems.

Effect of sodium alginate block type on the physicochemical properties and curcumin release behavior of quaternized chitosan-oxidized sodium alginate Schiff base hydrogels.

Controlling bioactive ingredients release by modulating the 3D network structure of cross-linked hydrogels is important for functional food development. Hereby, oxidized sodium alginate (OSA) with varying aldehyde contents was formed by periodate oxidation of sodium alginate (SA) with different ß-d-mannuronic acid (M) and α-l-guluronic acid (G) ratios (M/G = 1:2, 1:1, and 2:1) and its structure was characterized. Moreover, hydrogels were prepared via Schiff base and electrostatic interactions between quaternized chitosan (QCS) and OSA. The properties of hydrogels such as microstructure, thermal stability, swelling and controlled release were investigated. The results showed that OSA with M/G = 1:2 had the highest content of aldehyde groups, and the hydrogel formed by it and QCS had higher thermal stability and a denser network structure with the lowest equilibrium swelling rate, which could better control the release of curcumin. Additionally, it had good self-healing and can recover rapidly after the rupture of its network structure.

Self-assembly and aggregation behavior of temperature-controlled modified glycinin and d-galactose colloidal particles.

The molecular structure and morphologies of complex colloidal particles with modified glycine (S-11S) and d-galactose were studied by multispectral, microscopic imaging and chromatographic techniques at different temperatures, and the self-assembly and aggregation mechanisms were determined. Overall, high-temperature-treated S-11S and d-galactose associate at cysteine and phenylalanine sites and self-assemble into colloidal particles of greater stability than glycinin and S-11S via ionic and disulfide bonds. The structure and subunit content of composite colloidal particles were changed. Assessing the sub-microstructure reveals that temperature can regulate the directional aggregation of complex colloidal particles. The elasticity of the complex colloidal particles is maximum enhanced at 95 ℃ as confirmed by the rheological. Thus, the heat-treated aggregation of the soy protein and its complex was evaluated to provide a new theoretical basis for the application of soy protein in gels and other areas and contribute to the design of new soy protein products.

Casein-phosphatidylcholine emulsifier remodels LPS-induced intestinal barrier disfunction via regulating ferroptosis and lipid metabolism.

Recently, the biosafety of synthetic emulsifier in intestinal barrier has raised significant concerns. Casein- phosphatidylcholine (CP), which is a natural emulsifier, has better emulsification and stability. However, the effect of CP on intestinal barrier remains unknow. Intestinal permeability and lipomics analysis showed that carboxymethyl cellulose (CMC) and CP have no significant effect on intestinal barrier in normal intestinal barrier model, whereas CP increased transmembrane resistance value and remodeled lipid homeostasis in LPS induced intestinal barrier dysfunction model, indicating its superior biosafety. To explore the underlying molecular mechanism of emulsifier on intestinal barrier dysfunction, the bioinformatics analysis of six original microarray datasets including 168 cases in NCBI-Gene Expression Omnibus database showed ferroptosis-related genes showed a significant differential expression. The quantitative polymerase chain reaction analysis demonstrated that CP can repair the imbalance of lipid homeostasis induced by LPS and restore normal intestinal permeability by regulating the expression of ferroptosis-related genes, while CMC could can enhance intestinal permeability by inducing ferroptosis of intestinal epithelial cells through lipid peroxidation. In conclusion, this study highlighted CP could remodel LPS-induced intestinal barrier disfunction via regulating ferroptosis and lipid metabolism. These findings can be used as a new insight for the design of new healthy emulsifier.

Comparison of pH-induced protein-polyphenol self-assembly methods: Binding mechanism, structure, and functional characteristics.

Herein, we used pH-shifted and pH-driven methods to assemble kidney-bean protein isolate (KPI) and luteolin (Lut) into a nanocomplex and subsequently investigated their binding mechanism, structure, and functional properties. Results showed that the nanocomplex prepared by the pH-driven method exhibited a better encapsulation effect and controlled release of Lut. Fluorescence spectroscopy and molecular docking analysis showed that the binding affinities under alkaline conditions were higher than those under acidic and neutral conditions. Various spectral techniques were used to determine the structural changes in the KPI-Lut nanocomplex, including the transformation of α-helices and ß-sheets and alteration of specific amino acid microenvironments, which were more pronounced in the pH-driven nanocomplex. The structural changes in the nanocomplex further affected their surface hydrophobicity and thermal stability. Additionally, the combination of KPI and Lut significantly improved the antioxidant activity and α-glucosidase inhibitory ability of the resultant nanocomplexes, particularly the one prepared by the pH-driven method.

Changes in the structure and functional properties of soybean isolate protein: Effects of different modification methods.

Soybean protein isolate (SPI) is an important plant protein in food processing; however, its spherical structure prevents the exposure of its hydrophobic residues and affects its functional properties. In this study, we elucidate the effects of deamidation, phosphorylation, and glycosylation on the structure (Fourier-transform infrared spectroscopy, circular dichroism, fluorescence, and scanning electron microscopy) and functional properties (solubility, emulsifying activity index (EAI), and emulsifying stability index (ESI)) of SPI. The zeta potentials of the deamidated, phosphorylated, and glycosylated (DSPI, PSPI, and MSPI, respectively) samples decreased significantly (p < 0.05) relative to those of SPI. The functional properties of the modified SPI samples were improved, with MSPI-2 showing the best solubility (86.73 ± 0.34%), EAI (118.89 ± 0.73 m2/g), and ESI (273.33 ± 0.59 min). Moreover, the effects of the three modifications on the SPI functional properties increase in the order MSPI > PSPI > DSPI. These results provide a theoretical understanding the relationship between the modifications and SPI structure.

Curcumin-loaded oil body emulsions prepared by an ultrasonic and pH-driven method: Fundamental properties, stability, and digestion characteristics.

In this study, oil bodies (OBs) loaded with curcumin (Cur) were successfully prepared via an ultrasonic and pH-driven method. Ultrasonic treatment significantly improved the encapsulation efficiency (EE) and loading capacity (LC) of Cur, producing OB particles with small size, uniform distribution, and high ζ-potential absolute values. When the ultrasonic power was 200 W, the EE, LC, and ζ-potential absolute value were the greatest (88.27 %, 0.044 %, and -25.71 mV, respectively), and the OBs possessed the highest yellowness, representing the best treatment result. The confocal laser scanning microscopy (CLSM) and cryo-scanning electron microscopy (cryo-SEM) results was also intuitionally shown that. Moreover, circular dichroism (CD) proved that ultrasonic treatment could unfold the surface protein structure, further enhancing the stability. Therefore, the cream index (CI), peroxide value (POV), and thiobarbituric acid reactive substances (TBARS) were the lowest when the ultrasonic power was 200 W. In this case, the Cur loaded in OBs was well protected against hostile conditions, evidenced by the highest Cur retention rate and the lowest degradation rate constant. Finally, the in vitro gastrointestinal digestion simulation results showed that the ultrasonic treatment effectively increased the release of FFA, bioaccessibility, and stability of Cur, especially when the ultrasonic power was 200 W. This research offers a new OB-based delivery system to stabilize, deliver, and protect Cur for food processing.

Construction of protein-, polysaccharide- and polyphenol-based conjugates as delivery systems.

Natural polymers, such as polysaccharides and proteins, have been used to prepare several delivery systems owing to their abundance, bioactivity, and biodegradability. They are usually modified or combined with small molecules to form the delivery systems needed to meet different needs in food systems. This paper reviews the interactions of proteins, polysaccharides, and polyphenols in the bulk phase and discusses the design strategies, coupling techniques, and their applications as conjugates in emulsion delivery systems, including traditional, Pickering, multilayer, and high internal-phase emulsions. Furthermore, it explores the prospects of the application of conjugates in food preservation, food development, and nanocarrier development. Currently, there are seven methods for composite delivery systems including the Maillard reaction, carbodiimide cross-linking, alkali treatment, enzymatic cross-linking, free radical induction, genipin cross-linking, and Schiff base chemical cross-linking to prepare binary and ternary conjugates of proteins, polysaccharides, and polyphenols. To design an effective target complex and its delivery system, it is helpful to understand the physicochemical properties of these biomolecules and their interactions in the bulk phase. This review summarizes the knowledge on the interaction of biological complexes in the bulk phase, preparation methods, and the preparation of stable emulsion delivery system.

Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms.

Herein, cationic soy protein (NSPI) was synthesized by grafting Ethylenediamine (EDA) onto soy protein isolate (SPI), and protein-gallic acid (GA) complexes were formed by mixing NSPI with GA in various ratios. We assessed the structure, particle size, thermal stability, emulsifying ability, and antioxidant capacity of NSPI and complexes. Results show that grafting with EDA introduced a positive charge to SPI and resulted in a uniform particle size, and enhanced thermal stability, emulsifying ability, and antioxidant capacity. In addition, NSPI presented more amino groups and stronger interactions with GA compared to SPI. EDA and GA synergistically increased the flexibility of SPI, reducing the α-helix content and increasing the random coil content. Moreover, the interactions between SPI, NSPI, and GA were static, and hydrophobic and electrostatic between GA and SPI and NSPI, respectively. Grafting SPI with EDA improved functionality and interactions with GA, implying that NSPI-GA complexes may function as emulsifiers and antioxidants.

Ultrasound-assisted preparation of protein-polyphenol conjugates and their structural and functional characteristics.

Herein, ultrasound-assisted conventional covalent binding methods (alkali treatment, free radical mediation, and an enzymatic method) were used to prepare soybean protein isolate (SPI)-(-)-epigallocatechin gallate (EGCG) conjugates to investigate the enhancement effect of the ultrasound synergistic treatment. In addition, the influence of EGCG grafting on the structure and properties of SPI was evaluated via reactive group analysis, spectral analysis, surface hydrophobicity measurements, emulsification property assessment, and α-glucosidase inhibition analysis. The obtained results revealed that the enzymatic method produced the highest polyphenol grafting content among the conventional techniques. Meanwhile, ultrasound treatment increased the amount of grafted polyphenol species during the alkali treatment and free radical mediation procedure, decreased the grafting efficiency in the enzymatic method, and maximized the grafting efficiency during the alkali treatment. In addition, reactive group and spectral analyses demonstrated that EGCG formed C-N and C-S bonds with SPI and decreased the α-helix content in the protein structure, thereby increasing the molecular flexibility of SPI. It also produced hydrogen bonds and hydrophobic interactions, as demonstrated by the results of molecular docking. Furthermore, the EGCG grafting of SPI conducted under the ultrasound-assisted conditions endowed SPI with unique functional characteristics, including good emulsification and antioxidant properties and high α-glucosidase inhibitory activity, while the ultrasound-assisted alkali treatment resulted in the optimal functional properties. The results of this study provide new insights into the effective preparation of SPI-EGCG complexes with multiple functionalities, thereby expanding the scope of high-value SPI utilization.

Ethanol as a switch to induce soybean lipophilic protein self-assembly and resveratrol delivery.

Protein-based nanoparticles or nanocarriers of emulsion systems have piqued the interest of nutrition and health care goods. As a result, this work examines the characterisation of ethanol-induced soybean lipophilic protein (LP) self-assembly for resveratrol (Res) encapsulation, particularly the influence on emulsification. By varying the ethanol content ([E]) in the range of 0-70% (v/v), the structure, size, and morphology of LP nanoparticles may be adjusted. Similarly, the self-assembled LPs have a strong [E] dependency on the encapsulation efficiency of Res. For [E] = 40% (v/v), Res had the highest encapsulation efficiency (EE) and load capacity (LC) of 97.1% and 141.0 µg/mg nanoparticles, respectively. Most of the Res was encapsulated by the hydrophobic core of LP. Moreover, for [E] = 40% (v/v), LP-Res showed significantly improved emulsifying properties, independent of low-oil or high-oil emulsion systems. Furthermore, the ethanol-induced production of appropriate aggregates increased emulsion system stability, hence increasing Res retention during storage.

Effects of homogeneous and ultrasonic treatment on casein/phosphatidylcholine complex-emulsions: Stability and bioactivity insights.

Casein (CAS), a typical protein emulsifier, has functional properties limited by its chemical structure in practical production applications. This study aimed to combine phosphatidylcholine (PC) and casein to form a stable complex (CAS/PC) and improve its functional properties through physical modification (homogeneous and ultrasonic treatment). To date, few studies have explored the effects of physical modification on the stability and biological activity of CAS/PC. Interface behavior analysis showed that compared to homogeneous treatment, PC addition and ultrasonic treatment could decrease the mean particle size (130.20 ± 3.96 nm) and increase the zeta potential (-40.13 ± 1.12 mV), indicating the emulsion is more stable. The chemical structural analysis of CAS showed that PC addition and ultrasonic treatment promoted changes in its sulfhydryl content and surface hydrophobicity, exposing more free sulfhydryl groups and hydrophobic binding sites, thereby enhancing its solubility and improving the stability of the emulsion. Additionally, storage stability analysis revealed that the incorporation of PC with ultrasonic treatment could improve the root mean square deviation value and radius of gyration value of CAS. These modifications resulted in an increase the binding free energy between CAS and PC (-238.786 kJ/mol) at 50 °C, leading to an improvement in the thermal stability of the system. Furthermore, digestive behavior analysis indicated that PC addition and ultrasonic treatment could increase the total FFA release from 667.44 ± 22.33 µmol to 1250.33 ± 21.56 µmol. In conclusion, the study underscores the effectiveness of PC addition and ultrasonic treatment in enhancing the stability and bioactivity of CAS, offering novel ideas for designing stable and healthy emulsifiers.

Foodomics revealed the effects of ultrasonic extraction on the composition and nutrition of cactus fruit (Opuntia ficus-indica) seed oil.

Cactus is a tropical fruit with a high nutritional value; however, little information is available regarding the comprehensive utilization of its byproducts. This study aimed to explore the composition and nutritional value of cactus fruit seed oil (CFO) and reveal the effects of ultrasound-assisted extraction and traditional solvent extraction on oil quality. Foodomics analysis showed that CFO extracted using a traditional solvent is rich in linolenic acid (9c12cC18:2, 57.46 ± 0.84 %), α-tocopherol (20.01 ± 1.86 mg/100 g oil), and canolol (200.10 ± 1.21 µg/g). Compared to traditional solvent extraction, ultrasound-assisted extraction can significantly increase the content of lipid concomitants in CFO, whereas excessive ultrasound intensity may lead to the oxidation of oils and the formation of free radicals. Analysis of the thermal properties showed that ultrasound had no effect on the crystallization or melting behavior of CFO. To further demonstrate the nutritional value of CFO, a lipopolysaccharide (LPS)-induced lipid metabolism imbalance model was used. Lipidomics analysis showed that CFO significantly reduced the content of oxidized phospholipids stimulated by LPS and increased the content of highly bioactive metabolites such as ceramides, thus alleviating LPS-induced damage in C. elegans. Hence, CFO is a functional oil with high value, and ultrasound-assisted extraction is advocated. These findings provide new insights into the comprehensive utilization of cactus fruits.

Effects of ultrasonic treatment on the structural and functional properties of cactus (Opuntia ficus-indica) seed protein.

With the steady increase in the consumption of ultra-processed foods, there is growing interest in sustainable diets that include more plant protein. However, little information is available regarding the structural and functional properties of cactus (Opuntia ficus-indica) seed protein (CSP), a by-product of the cactus seed food-processing chain. This study aimed to explore the composition and nutritional value of CSP and reveal the effects of ultrasound treatment on protein quality. Protein chemical structure analysis showed that an appropriate intensity of ultrasound treatment (450 W) could significantly increase protein solubility (96.46 ± 2.07%) and surface hydrophobicity (13.76 ± 0.85 µg), decrease the content of T-SH (50.25 ± 0.79 µmol/g) and free-SH (8.60 ± 0.30 µmol/g), and enhance emulsification characteristics. Circular dichroism analysis further confirmed that the ultrasonic treatment increased the α-helix and random coil content. Amino acid analysis also suggested that ultrasound treatment (450 W) increased the hydrophobic amino acid content. To evaluate the impact of changes in the chemical structure, its digestion behavior was studied. The results showed that ultrasound treatment increased the release rate of free amino acids. Furthermore, nutritional analysis showed that the digestive products of CSP by ultrasound treatment can significantly enhance the intestinal permeability, increase the expression of ZO-1, Occludin and Claudin-1, thus repairing LPS induced intestinal barrier disfunction. Hence, CSP is a functional protein with high value, and ultrasound treatment is recommended. These findings provide new insights into the comprehensive utilization of cactus fruits.

Improving the biological activity, functional properties, and emulsion stability of soybean meal hydrolysate via covalent conjugation with polyphenol.

The use of by-products as functional components in food production is gaining popularity. This study investigated the structure, biological activity, interaction force, and emulsion stability of soybean meal hydrolysate (SMHs) after covalent conjugation with proanthocyanidin (PC), epigallocatechin (EGCG), gallic acid (GA), and caffeic acid (CA). SDS-PAGE confirmed the formation of SMHs-polyphenol conjugates. Structural analysis indicates unfolding and disordered-structure formation. This transformation directly influenced the antioxidant activity and emulsification of SMHs. The antioxidant and emulsifying properties of all covalent complexes were superior to SMHs, in order of SMHs-PC, SMHs-EGCG, SMHs-GA, and SMHs-CA. Among, SMHs-PC conjugates displayed the highest antioxidant activity (ABTS•+ and DPPH radical scavenging capacities of 89.33% and 52.71%, respectively), total polyphenol content (235.10 mg/g), and emulsification activity (EAI) and stability (ESI) values (109.27 m2/g and 135.05 min, respectively). Moreover, SMHs-PC emulsion showed the smallest particle size (467.20 nm), highest viscosity (520.19 Pa.s), highest protein adsorption (94.33%), and lowest release rate of free fatty acids (FFAs) (18.61%) after digestion. These results provided valuable information for the use of modified SMHs as emulsifiers, which is a promising approach for increasing the value of soybean meal.

Ultrasound-assisted alkali removal of proteins from wastewater generated during oil bodies extraction.

In this study, an ultrasonic-assisted alkaline method was used to remove proteins from wastewater generated during oil-body extraction, and the effects of different ultrasonic power settings (0, 150, 300, and 450 W) on protein recovery were investigated. The recoveries of the ultrasonically treated samples were higher than those of the samples without ultrasonic treatment, and the protein recoveries increased with increasing power, with a protein recovery of 50.10 % ± 0.19 % when the ultrasonic power was 450 W. Amino acid analysis showed that the amino acids comprising the recovered samples were consistent, regardless of the ultrasonic power used, but significant differences in the contents of amino acids were observed. No significant changes were observed in the protein electrophoretic profile using dodecyl polyacrylamide gel, indicating that sonication did not change the primary structures of the recovered samples. Fourier transform infrared and fluorescence spectroscopy revealed that the molecular structures of the samples changed after sonication, and the fluorescence intensity increased gradually with increasing sonication power. The contents of α-helices and random coils obtained at an ultrasonic power of 450 W decreased to 13.44 % and 14.31 %, respectively, whereas the ß-sheet content generally increased. The denaturation temperatures of the proteins were determined using differential scanning calorimetry, and ultrasound treatment reduced the denaturation temperatures of the samples, which was associated with the structural and conformational changes caused by their chemical bonding. The solubility of the recovered protein increased with increasing ultrasound power, and a high solubility was essential in good emulsification. The emulsification of the samples was improved well. In conclusion, ultrasound treatment changed the structure and thus improved the functional properties of the protein.