Near-infrared spectroscopy to quantify overall thermal process intensity during high-moisture extrusion of soy protein concentrate.

High-moisture extrusion (HME) is widely used to produce meat analogues. During HME the plant-based materials experience thermal and mechanical stresses. It is complicated to separate their effects on the final products because these effects are interrelated. In this study we hypothesize that the intensity of the thermal treatment can explain a large part of the physicochemical changes that occur during extrusion. For this reason, near-infrared (NIR) spectroscopy was used as a novel method to quantify the thermal process intensity during HME. High-temperature shear cell (HTSC) processing was used to create a partial least squares (PLS) regression curve for processing temperature under controlled processing conditions (root mean standard error of cross-validation (RMSECV) = 4.00 °C, coefficient of determination of cross-validation (R2CV) = 0.97). This PLS regression model was then applied to HME extrudates produced at different screw speeds (200-1200 rpm) and barrel temperatures (100-160 °C) with two different screw profiles to calculate the equivalent shear cell temperature as a measure for thermal process intensity. This equivalent shear cell temperature reflects the effects of changes in local temperature conditions, residence time and thermal stresses. Furthermore, it can be related to the degree of texturization of the extrudates. This information can be used to gain new insights into the effect of various process parameters during HME on the thermal process intensity and extrudate quality.

Differential effects of heating modes on the immunogenic potential of soy-derived peptides released after in vitro infant digestion.

During production of soy-based infant formula, soy protein undergoes heating processes. This study investigated the differential impact of heating modes on the immunogenic potential of peptides in soy protein digests. Wet or dry heating was applied, followed by in vitro gastrointestinal infant digestion. The released peptides were analyzed by LC-MS/MS. Bioinformatics tools were utilized to predict and identify potential linear B-cell and T-cell epitopes, as well as to explore cross-reactivity with other legumes. Subsequently, the peptide intensities of the same potential epitope across different experimental conditions were compared. As a result, we confirmed the previously observed enhancing effect of wet heating on infant digestion and inhibitory effect of dry heating. A total of 8,546 peptides were detected in the digests, and 6,684 peptides were with a score over 80. Among them, 29 potential T-cell epitopes and 27 potential B-cell epitopes were predicted. Cross-reactivity between soy and other legumes, including peanut, pea, chickpea, lentil, kidney bean, and lupine, was also detected. Overall, heating and digestion time could modulate the potential to trigger peptide-induced immune responses.

Characterization of high-internal-phase emulsions based on soy protein isolate with varying concentrations of soy hull polysaccharide and their capabilities for probiotic delivery: In vivo and in vitro release and thermal stability.

In this study, the impact of soy hull polysaccharide (SHP) concentration on high-internal-phase emulsions (HIPEs) formation and the gastrointestinal viability of Lactobacillus plantarum within HIPEs were demonstrated. Following the addition of SHP, competitive adsorption with soy protein isolate (SPI) occurred, leading to increased protein adhesion to the oil-water interface and subsequent coating of oil droplets. This process augmented viscosity and enhanced HIPEs stability. Specifically, 1.8 % SHP had the best encapsulation efficiency and delivery efficiency, reaching 99.3 % and 71.1 %, respectively. After 14 d of continuous zebrafishs feeding, viable counts of Lactobacillus plantarum and complex probiotics in the intestinal tract was 1.1 × 107, 1.3 × 107, respectively. In vitro experiments further proved that HIPEs' ability to significantly enhance probiotics' intestinal colonization and provided targeted release for colon-specific delivery. These results provided a promising strategy for HIPEs-encapsulated probiotic delivery systems in oral food applications.

The impact of extraction processes on the physicochemical, functional properties and structures of bamboo shoot protein.

This study aimed to extract bamboo shoot protein (BSP) using different extraction approaches and compare their functional and physicochemical properties with commercial protein ingredients, including whey protein and soy protein isolates. The extraction methods including alkali extraction (AE), salt extraction (SE), and phosphate-aided ethanol precipitation (PE) were used. An enhanced solvent extraction method was utilized in combination, resulting in a significant improvement in the protein purity, which reached 81.59 %, 87.36 %, and 67.08 % respectively. The extraction methods had significant effects on the amino acid composition, molecular weight distribution, and functional properties of the proteins. SE exhibited the best solubility and emulsification properties. Its solubility reached up to 93.38 % under alkaline conditions, and the emulsion stabilized by SE with enhanced solvent extraction retained 60.95 % stability after 120 min, which could be attributed to its higher protein content, higher surface hydrophobicity, and relative more stable and organized protein structure. All three BSP samples demonstrated better oil holding capacity, while the SE sample showed comparable functional properties to soy protein such as foaming and emulsifying properties. These findings indicate the potential of BSP as an alternative plant protein ingredient in the food industry.

Enhancing storage and gastroprotective viability of Lactiplantibacillus plantarum encapsulated by sodium caseinate-inulin-soy protein isolates composites carried within carboxymethyl cellulose hydrogel.

Probiotics are subjected to various edible coatings, especially proteins and polysaccharides, which serve as the predominant wall materials, with ultrasound, a sustainable green technology. Herein, sodium caseinate, inulin, and soy protein isolate composites were produced using multi-frequency ultrasound and utilized to encapsulateLactiplantibacillus plantarumto enhance its storage, thermal, and gastrointestinal viability. The physicochemical analyses revealed that the composites with 5 % soy protein isolate treated with ultrasound at 50 kHz exhibited enough repulsion forces to maintain stability, pH resistance, and the ability to encapsulate larger particles and possessed the highest encapsulation efficiency (95.95 %). The structural analyses showed changes in the composite structure at CC, CH, CO, and amino acid residual levels. Rheology, texture, and water-holding capacity demonstrated the production of soft hydrogels with mild chewing and gummy properties, carried the microcapsules without coagulation or sedimentation. Moreover, the viability attributes ofL. plantarumevinced superior encapsulation, protecting them for at least eight weeks and against heat (63 °C), reactive oxidative species (H2O2), and GI conditions.

Soybean isolate protein complexes with different concentrations of inulin by ultrasound treatment: Structural and functional properties.

The effects of ultrasound and different inulin (INU) concentrations (0, 10, 20, 30, and 40 mg/mL) on the structural and functional properties of soybean isolate protein (SPI)-INU complexes were hereby investigated. Fourier transform infrared spectroscopy showed that SPI was bound to INU via hydrogen bonding. All samples showed a decreasing and then increasing trend of α-helix content with increasing INU concentration. SPI-INU complexes by ultrasound with an INU concentration of 20 mg/mL (U-2) had the lowest content of α-helix, the highest content of random coils and the greatest flexibility, indicating the proteins were most tightly bound to INU in U-2. Both UV spectroscopy and intrinsic fluorescence spectroscopy indicated that it was hydrophobic interactions between INU and SPI. The addition of INU prevented the exposure of tryptophan and tyrosine residues to form a more compact tertiary structure compared to SPI alone, and ultrasound caused further unfolding of the structure of SPI. This indicated that the combined effect of ultrasound and INU concentration significantly altered the tertiary structure of SPI. SDS-PAGE and Native-PAGE displayed the formation of complexes through non-covalent interactions between SPI and INU. The ζ-potential and particle size of U-2 were minimized to as low as -34.94 mV and 110 nm, respectively. Additionally, the flexibility, free sulfhydryl groups, solubility, emulsifying and foaming properties of the samples were improved, with the best results for U-2, respectively 0.25, 3.51 µmoL/g, 55.51 %, 269.91 %, 25.90 %, 137.66 % and 136.33 %. Overall, this work provides a theoretical basis for improving the functional properties of plant proteins.

Homologous Overexpression of Tyrosinase in Trichoderma reesei and Its Application in Glycinin Cross-Linking.

Tyrosinase is capable of oxidizing tyrosine residues in proteins, leading to intermolecular protein cross-linking, which could modify the protein network of food and improve the texture of food. To obtain the recombinant tyrosinase with microbial cell factory instead of isolation tyrosinase from the mushroom Agaricus bisporus, a TYR expression cassette was constructed in this study. The expression cassette was electroporated into Trichoderma reesei Rut-C30 and integrated into its genome, resulting in a recombinant strain C30-TYR. After induction with microcrystalline cellulose for 7 days, recombinant tyrosinase could be successfully expressed and secreted by C30-TYR, corresponding to approximately 2.16 g/L tyrosinase in shake-flask cultures. The recombinant TYR was purified by ammonium sulfate precipitation and gel filtration, and the biological activity of purified TYR was 45.6 U/mL. The purified TYR could catalyze the cross-linking of glycinin, and the emulsion stability index of TYR-treated glycinin emulsion was increased by 30.6% compared with the untreated one. The cross-linking of soy glycinin by TYR resulted in altered properties of oil-in-water emulsions compared to emulsions stabilized by native glycinin. Therefore, cross-linking with this recombinant tyrosinase is a feasible approach to improve the properties of protein-stabilized emulsions and gels.

Understanding the foam stability mechanisms of complex formed by soy protein isolate and different charged polysaccharides: Air/water interfacial behavior and rheological characteristics.

This study evaluated the foaming properties, the dynamic adsorption behavior at the air/water (A/W) interface and the foam rheological characteristics of complexes formed by soy protein isolate (SPI) and different charged polysaccharides, including chitosan (CS), guar gum (GUG) and gellan gum (GEG). The results showed that the SPI/CS10 had the highest initial foam volume (26.67 mL), which were 3.89 %, 100.08 % and 70.19 % higher than that of single SPI, SPI/GUG and SPI/GEG complexes, respectively. Moreover, three charged polysaccharides could all significantly improve the foam stability of complexes. Among them, foams stabilized by SPI/GEG10 were the most stable that the foam volume slightly changed (approximately 1 mL) and no drainage occurred throughout the whole recording process. The interfacial behavior analysis showed that SPI/CS10 had higher diffusion (Kdiff) and rearrangement rate (KR) but lower penetration rate (KP) at the A/W interface compared with single SPI, while SPI/GUG10 and all SPI/GEG complexes showed higher KR and KP but lower Kdiff. In addition, SPI/CS10 was beneficial to concurrently enhance the elastic strength and solid-like behavior of foam system, while all SPI/GEG complexes could improve the elastic strength of foam system but was not conducive to the solid-like behavior.

Mechanism of l-cysteine-induced fibrous structural changes of soybean protein at different high-moisture extrusion zones.

In this study, the fibrous structure formation mechanism of soybean protein during high moisture extrusion processing was investigated using a dead-stop operation, and based on the interaction between soybean protein concentrate (SPC) and L-cysteine (CYS). The thermal properties, SDS-PAGE and particle size distribution of the samples from different extrusion zones were investigated. It was revealed that the addition of a moderate amount of CYS (0.1 %) promoted the fibrous structure formation in the SPC extrudates and optimised the textural properties of the SPC extrudates. In the extruder barrel, addition of CYS (0.1 %) promoted protein depolymerisation and unfolding in the mixing and cooking zones, and facilitated protein aggregation in the die and cooling zones. Protein solubility and raman spectroscopy revealed that disulfide bonds were principally responsible for fibrous structure formation; favoured when the intermolecular disulfide bonds (t-g-t mode) was increased. Finally, the transformation of protein conformation was revealed by secondary structure and surface hydrophobicity, which confirmed that the effect of CYS on protein conformation mainly occurred in the cooling zone. This study provides a theoretical basis for the application of CYS to regulate the fibrous structure of meat analogues.

Effect of montmorillonite (MMT) on the properties of soybean meal protein isolate-based nanocomposite film loaded with debittered kinnow peel powder.

The synthetic, non-renewable nature and harmful effects of plastic packaging have led to the synthesis of eco-friendly renewable bio-nanocomposite film. The present work was aimed at the formulation and characterization of bio-nanocomposite film using soybean meal protein, montmorillonite (MMT), and debittered kinnow peel powder. The composition of film includes protein isolate (5% w/v), glycerol (50% w/w), peel powder (20% w/w), and MMT (0.5-2.5% w/w). Incorporation of MMT in soybean meal protein-based film loaded with kinnow peel powder showed lesser solubility (16.76-26.32%), and swelling ability (142.77-184.21%) than the film prepared without MMT (29.41%, & 229.41%, respectively). The mechanical properties like tensile strength of nanocomposite film improved from 9.41 to 38.69% with the increasing concentration of MMT. The water vapor transmission rate of the nanocomposite film was decreased by 3.45-17.85% when the MMT concentration increased. Fourier-transform infrared spectroscopy and X-ray diffraction analysis showed no considerable change in the structural properties of the film after the addition of MMT. Differential scanning colorimeter analysis revealed the increment in melting temperature (85.33-92.67 °C) of the film with a higher concentration of MMT. Scanning electron microscopy analysis indicated an increased distributed area of MMT throughout the film at higher concentrations. The antimicrobial activity of the film was remarkably increased by 4.96-17.18% with the addition of MMT. The results obtained in the current work confirmed that MMT incorporation in soybean meal protein-based film can augment its properties and can be utilized for enhancing the storage period of food products.

pH-regulated Tannic acid and soybean protein isolate adhesive for enhanced performance in plant-based meat analogues.

A food adhesive comprising tannic acid (TA) and soybean protein isolate (SPI) was developed to establish a cohesive bond between soy protein gel and simulated fat. The impact of varying TA concentrations and pH levels on the adhesive's rheology, thermal stability, chemical structure, and tensile strength were investigated. Rheological results revealed a gradual decrease in adhesive viscosity with increasing TA content. Differential scanning calorimetry (DSC) and thermal gravimetric (TG) results indicated that the stability of the adhesive improved with higher TA concentrations, reaching its peak at 0.50% TA addition. The incorporation of TA resulted in the cross-linking of amino group in unfolded SPI molecules, forming a mesh structure. However, under alkaline conditions (pH 9), adhesive viscosity and stability increased compared to the original pH. This shift was due to the disruption of the SPI colloidal charge structure, an increase in the stretching of functional groups, further unfolding of the structure, and an enhanced binding of SPI to TA. Under the initial pH conditions, SPI reacted with TA's active site to form covalent crosslinked networks and hydrogen bonds. In alkaline condition, beyond hydrogen and ionic bonding, the catechol structure was oxidized, forming an ortho-quinone that crosslinked SPI and created a denser structure. Tensile strength measurements and freeze-thaw experiments revealed that the adhesive exhibited maximum tensile strength and optimal adhesion with 0.75% TA at pH 9, providing the best overall performance. This study provides a new formulation and approach for developing plant-based meat analogues adhesives.

A self-healing crosslinked-xanthan gum/soy protein based film containing halloysite nanotube and propolis with antibacterial and antioxidant activity for wound healing.

Traumatic multidrug-resistant bacterial infections are the most threat to wound healing. Lower extremity wounds under diabetic conditions display a significant delay during the healing process. To overcome these challenges, the utilization of protein-based nanocomposite dressings is crucial in implementing a successful regenerative medicine approach. These dressings hold significant potential as polymer scaffolds, allowing them to mimic the properties of the extracellular matrix (ECM). So, the objective of this study was to develop a nanocomposite film using dialdehyde-xanthan gum/soy protein isolate incorporated with propolis (PP) and halloysite nanotubes (HNTs) (DXG-SPI/PP/HNTs). In this protein-polysaccharide hybrid system, the self-healing capability was demonstrated through Schiff bonds, providing a favorable environment for cell encapsulation in the field of tissue engineering. To improve the properties of the DXG-SPI film, the incorporation of polyphenols found in PP, particularly flavonoids, is proposed. The synthesized films were subjected to investigations regarding degradation, degree of swelling, and mechanical characteristics. Additionally, halloysite nanotubes (HNTs) were introduced into the DXG-SPI/PP nanocomposite films as a reinforcing filler with varying concentrations of 3 %, 5 %, and 7 % by weight. The scanning electron microscope (SEM) analysis confirmed the proper embedding and dispersion of HNTs onto the DXG-SPI/PP nanocomposite films, leading to functional interfacial interactions. The structure and crystallinity of the synthesized nanocomposite films were characterized using Fourier Transform Infrared Spectrometry (FTIR) and X-ray diffraction (XRD), respectively. Moreover, the developed DXG-SPI/PP/HNTs nanocomposite films significantly improved cell growth of NIH-3T3 fibroblast cells in the presence of PP and HNTs, indicating their cytocompatibility. The antibacterial activity of the nanocomposite was evaluated against Escherichia coli (E. Coli) and Staphylococcus aureus (S. Aureus), which are commonly associated with wound infections. Overall, our findings suggest that the synthesis of DXG-SPI/PP/HNTs nanocomposite scaffolds holds great promise as a clinically relevant biomaterial and exhibits strong potential for numerous challenging biomedical applications.

Localization of G1A1a Allergenic Domain Destroyed by Thermal Processing.

Glycinin is an important allergenic protein. A1a is the acidic chain of the G1 subunit in glycinin (G1A1a), and it has strong allergenicity. In this study, we used phage display technology to express the protein of G1A1a and its overlapping fragments and an indirect enzyme-linked immunosorbent assay (iELISA) to determine the antigenicity and allergenicity of the expressed protein. After three rounds of screening, it was determined that fragment A1a-2-B-I (151SLENQLDQMPRRFYLAGNQEQEFLKYQQEQG181) is the allergenic domain of G1A1a destroyed by thermal processing. In addition, three overlapping peptides were synthesized from fragments A1a-2-B-I, and a linear epitope was found in this domain through methods including dot blot and iELISA. Peptide 2 (157DQMPRRFYLANGNQE170) showed allergenicity, and after replacing it with alanine, it was found that amino acids D157, Q158, M159, and Y164 were the key amino acids that affected its antigenicity, while Q158, M159, R162, and N168 affected allergenicity.

Deciphering the interaction mechanism between soy protein isolate and fat-soluble anthocyanin on experiments and molecular simulations.

In this work, the acylated anthocyanin (Ca-An) was prepared by enzymatic modification of black rice anthocyanin with caffeic acid, and the binding mechanism of Ca-An to soybean protein isolate (SPI) was investigated by experiments and computer simulation to expand the potential application of anthocyanin in food industry. Multi-spectroscopic studies revealed that the stable binding of Ca-An to SPI induced the folding of protein polypeptide chain, which transformed the secondary structure of SPI trended to be flexible. The microenvironment of protein was transformed from hydrophobic to hydrophilic, while tyrosine played dominant role in quenching process. The binding sites and forces of the complexes were determined by computer simulation for further explored. The protein conformation of the 7S and 11S binding regions to Ca-An changed, and the amino acid microenvironment shifted to hydrophilic after binding. The results showed that more non-polar amino acids existed in the binding sites, while in binding process van der Waals forces and hydrogen bonding played a major role hydrophobicity played a minor role. Based on MM-PBSA analysis, the binding constants of 7S-Ca-An and 11S-Ca-An were 0.518 × 106 mol-1 and 5.437 × 10-3 mol-1, respectively. This information provides theoretical guidance for further studying the interaction between modified anthocyanins and biomacromolecules.

Molecular modification of low-dissolution soy protein isolates by anionic xanthan gum, neutral guar gum, or neutral konjac glucomannan to improve the protein dissolution and stabilize fish oil emulsion.

Herein, the effects of anionic xanthan gum (XG), neutral guar gum (GG), and neutral konjac glucomannan (KGM) on the dissolution, physicochemical properties, and emulsion stabilization ability of soy protein isolate (SPI)-polysaccharide conjugates were studied. The SPI-polysaccharide conjugates had better water dissolution than the insoluble SPI. Compared with SPI, SPI-polysaccharide conjugates had lower ß-sheet (39.6 %-56.4 % vs. 47.3 %) and α-helix (13.0 %-13.2 % vs. 22.6 %) percentages, and higher ß-turn (23.8 %-26.5 % vs. 11.0 %) percentages. The creaming stability of SPI-polysaccharide conjugate-stabilized fish oil-loaded emulsions mainly depended on polysaccharide type: SPI-XG (Creaming index: 0) > SPI-GG (Creaming index: 8.1 %-21.2 %) > SPI-KGM (18.1 %-40.4 %). In addition, it also depended on the SPI preparation concentrations, glycation times, and glycation pH. The modification by anionic XG induced no obvious emulsion creaming even after 14-day storage, which suggested that anionic polysaccharide might be the best polysaccharide to modify SPI for emulsion stabilization. This work provided useful information to modify insoluble proteins by polysaccharides for potential application.

Conformation-Activity Mechanism of Alcalase Hydrolysis for Reducing In Vitro Allergenicity of Instant Soy Milk Powder.

Effective reduction of the allergenicity of instant soy milk powder (ISMP) is practically valuable for expanding its applications. This study optimized the enzymolysis technology of ISMP using single-factor experiments and response surface methodology, combined serological analysis, cellular immunological models, bioinformatics tools, and multiple spectroscopy techniques to investigate the effects of alcalase hydrolysis on allergenicity, spatial conformation, and linear epitopes of ISMP. Under the optimal process, special IgE and IgG1 binding abilities and allergenic activity to induce cell degranulation of alcalase-hydrolyzed ISMP were reduced by (64.72 ± 1.76)%, (56.79 ± 3.72)%, and (73.3 ± 1.19)%, respectively (P < 0.05). Moreover, the spatial conformation of instant soy milk powder hydrolysates (ISMPH) changed, including decreased surface hydrophobicity, a weaker peak of amide II band, lower contents of α-helix and ß-sheet, and an enhanced content of random coil. Furthermore, the linear epitopes of major soy allergens, 9 from glycinin and 13 from ß-conglycinin, could be directionally disrupted by alcalase hydrolysis. Overall, the structure-activity mechanism of alcalase hydrolysis to reduce ISMP allergenicity in vitro was preliminarily clarified. It provided a new research direction for the breakthrough in the desensitization of ISMP and a theoretical basis for revealing the potential mechanism of alcalase enzymolysis to reduce the allergenicity of ISMP.

Modification mechanism of soybean protein isolate-soluble soy polysaccharide complex by EGCG through covalent and non-covalent interaction: Structural, interfacial, and functional properties.

Soybean protein isolate was modified with polysaccharides and polyphenols to prepare a natural emulsifier with antioxidant capacity. Physicochemical, structural, interfacial, and functional properties of SPI-SSPS complex were investigated after covalent and non-covalent interacted with EGCG. SPI-SSPS-EGCG ternary complex with low EGCG concentrations (0.0625 and 0.125 mg/mL) showed a significant increase in absolute potential value and a decrease in turbidity. EGCG destroyed the original rigid structure of SPI-SSPS complex, and the covalent complexes had an ordered structure, while the non-covalent interaction resulted in disordered. The ternary complex with high EGCG concentrations (0.25 and 0.5 mg/mL) exhibited stronger EGCG binding capacity and lower surface hydrophobicity, which in turn affected its interfacial properties. The EAI and ESI of SPI-SSPS-EGCG covalent complex increased significantly, while the non-covalent complex had a significant change in EAI but no significant change in ESI with increasing EGCG concentration. The ternary complex showed significantly enhanced antioxidant capacity. The SPI-SSPS-EGCG ternary complex, with excellent antioxidant capacity and emulsifying property, making it suitable for emulsion delivery systems.

Rapid quantitative analysis of soybean protein isolates secondary structure by two-dimensional correlation infrared spectroscopy through pH perturbation.

The infrared spectroscopy (IR) signal of protein is prone to being covered by impurity signals, and the accuracy of the secondary structure content calculated using spectral data is poor. To tackle this challenge, a rapid high-precision quantitative model for protein secondary structure was proposed. Firstly, a two-dimensional correlation calculation was performed based on 60 groups of soybean protein isolates (SPI) infrared spectroscopy data, resulting in a two-dimensional correlation infrared spectroscopy (2DCOS-IR). Subsequently, the optimal characteristic bands of the four secondary structures were extracted from the 2DCOS-IR. Ultimately, partial least squares (PLS), long short-term memory (LSTM), and bidirectional long short-term memory (BILSTM) algorithms were used to model the extracted characteristic bands and predict the content of SPI secondary structure. The findings suggested that BILSTM combined with 2DCOS-IR model (2DCOS-BILSTM) exhibited superior predictive performance. The prediction sets for α-helix, ß-sheet, ß-turn, and random coil were designated as 0.9257, 0.9077, 0.9476, and 0.8443, respectively, and their corresponding RMSEP values were 0.26, 0.48, 0.20, and 0.15. This strategy enhances the precision of IR and facilitates the rapid identification of secondary structure components within SPI, which is vital for the advancement of protein industrial production.

Hawthorn pectin/soybean isolate protein hydrogel bead as a promising ferrous ion-embedded delivery system.

In this study, hydrogel beads [SPI/HP-Fe (II)] were prepared by cross-linking soybean isolate protein (SPI) and hawthorn pectin (HP) with ferrous ions as a backbone, and the effects of ultrasound and Fe2+ concentration on the mechanical properties and the degree of cross-linking of internal molecules were investigated. The results of textural properties and water-holding capacity showed that moderate ultrasonic power and Fe2+ concentration significantly improved the stability and water-holding capacity of the hydrogel beads and enhanced the intermolecular interactions in the system. Scanning electron microscopy (SEM) confirmed that the hydrogel beads with 60% ultrasonic power and 8% Fe2+ concentration had a denser network. X-ray photoelectron spectroscopy (XPS) and atomic absorption experiments demonstrated that ferrous ions were successfully loaded into the hydrogel beads with an encapsulation efficiency of 82.5%. In addition, in vitro, simulated digestion experiments were performed to understand how the encapsulated Fe2+ is released from the hydrogel beads, absorbed, and utilized in the gastrointestinal environment. The success of the experiments demonstrated that the hydrogel beads were able to withstand harsh environments, ensuring the bioactivity of Fe2+ and improving its bioavailability. In conclusion, a novel and efficient ferrous ion delivery system was developed using SPI and HP, demonstrating the potential application of SPI/HP-Fe (II) hydrogel beads as an iron supplement to overcome the inefficiency of intake of conventional iron supplements.

Establishing a novel ternary complex of soybean protein isolated-tannic acid-magnesium ion and its properties.

A ternary complex composed of soybean protein isolated (SPI), tannic acid (TA) and magnesium ion (M) was established to enhance the capability of protein carriers for TA delivery. SPI was firstly covalently bind with TA (TA-SPI) and then M was employed to form the ternary complex (M-TA-SPI). Their structures, gel and digestion properties were further investigated. TA was observed to covalently bind with SPI. TA-SPI and M-TA-SPI complexes showed different molecule size and spatial structures after binding with M and TA. The increasing of TA amount changed the intramolecular interactions, microstructure and texture properties of M-TA-SPI gels. Compared with TA-SPI, M retarded the gastric digestion of M-TA-SPI and caused higher TA release amount in intestinal tract. In this study, M-TA-SPI was determined to be a good carrier to protect and release TA in gastrointestinal digestion. This kind of complex may have potential applications for loading polyphenols in nutraceuticals.