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A soybean protein isolate (SPI)-based hydrogel with controllable properties was prepared under mild conditions using a simple mixing method with dialdehyde sodium alginate (DSA) as an eco-friendly macromolecular crosslinker. DSA was successfully synthesized via periodate oxidation. Analysis of the structure of the SPI/DSA hydrogel indicated that a 3D network was formed between SPI and DSA through dynamic imine and hydrogen bonds. The analysis of the physicochemical properties of the hydrogels showed that the micropore size, mechanical properties, and the swelling and release behavior of the hydrogels could be effectively regulated by changing the DSA content. When 3.0 wt% DSA was added, the hydrogel exhibited a dense and homogeneous network structure with optimal gel properties, which enabled the controlled release of curcumin. This effective structure is mainly attributed to the synergistic effect of short- and long-range chemical and physical crosslinking. Overall, the SPI/DSA hydrogels are effective carriers for the controlled release of bioactive compounds., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Improving the mechanical strength of protein freeze-dried gels materials has become a research priority in the field of nutrient delivery system development in recent years. In this study, double crosslinking freeze-dried gels were prepared by integrating laccase catalyzed sugar beet pectin (SBP) as a highly active filler molecule into the soybean isolate protein (SPI) thermally induced gel network, followed by freeze-drying. The double crosslinking freeze-dried gels were a porous material and the addition of SBP resulted in the formation of amorphous forms of freeze-dried gels with lower binding energy. The freeze-dried gels with 2.0 % SBP addition had the densest microstructure with the highest density (19.00 mg/cm 3 ) and mechanical strength (180.43 ± 15.27 KPa), and hydrogen bonding, NH, CN, and CO bands were the most important factors to maintain the freeze-dried gels structure. As the concentration of sugar beet pectin increased, the release mechanism of riboflavin underwent a shift from a Fickian to a non-Fickian diffusion mechanism. In addition, the highest bioavailability of riboflavin was found in the freeze-dried gels spiked with 2.0 % SBP. These results will contribute to the development of double crosslinking freeze-dried gels carriers for targeted slow release of hydrophilic bioactive., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have influenced the work reported in this article., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

In this study, the soybean protein isolate / chitosan oligosaccharide (SPI/COS) conjugates were developed using glycosylation and used as a stabilizer of carvacrol-loaded emulsions for refrigerating sea bass (Lateolabrax maculatus). The results of Fourier transform infrared spectroscopy and fluorescence spectroscopy showed that COS modified the secondary and tertiary structure of SPI by covalent binding. The SPI/COS conjugate with a mass ratio of SPI and COS of 4:1 (SPI/COS-4) exhibited high glycosylation degree, great water solubility and better emulsification properties. Carvacrol-loaded emulsion stabilized by the SPI/COS-4 (CE-SPI/COS-4) had nanoscale droplet size and remained stable during 40 days of storage. SPI/COS-4 aqueous solution (SPI/COS) and CE-SPI/COS-4 aqueous solution (CE-SPI/COS) in the form of immersion were applied to investigate their preservation effects on sea bass, with sterile water as control check (CK). Sea bass were stored at 4 °C and quality assessments of fish were performed periodically for up to 21 days, which included microbiological and physicochemical analysis. As suggested by microbiological analysis, CE-SPI/COS treatment could significantly inhibit the bacterial growth. The low total volatile basic nitrogen value, thiobarbituric acid value and K-value indicated that CE-SPI/COS greatly retarded protein and lipid oxidation in fish and significantly suppress the degradation of nucleotide. Moreover, fish treated with CE-SPI/COS had minimal color variation and water loss, and maintained hardness, adhesiveness, chewiness, and resilience of fish to the highest degree. Therefore, emulsions stabilized with SPI/COS conjugates may be employed as a potential strategy for the quality maintenance of sea bass., Competing Interests: Declaration of competing interest The authors declare that there is no conflict of interest., (Copyright © 2024 Elsevier B.V. All rights reserved.)

In this study, quercetin (Que) was encapsulated for controlled release during gastrointestinal digestion using zein-soy isolate protein (SPI) composite nanoparticles that were made following an antisolvent precipitation technique. The average particle size of the composite nanoparticles ranged from 182.1 to 230.9 nm, and the polydispersity index (PDI) was small (0.105-0.323). The microstructure revealed that the composite nanoparticles were spherically distributed and that Que. was embedded on the surface of the nanoparticles. Que. has an encapsulation efficiency of up to 93.3 %. Spectrum analysis, molecular docking and zeta potential measurements revealed that the interactions between the composite nanoparticles and Que. occurred mainly through hydrophobic interactions, hydrogen bonding, and electrostatic interactions. Compared with single zein nanoparticles, the composite nanoparticles showed a significant and controlled release of Que. during the whole simulated gastrointestinal digestion process. This study provides a novel method for the development of a controlled-release drug delivery system for controlling the release of Que., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

To improve the emulsion gel system of single soybean isolate protein (SPI) and to broaden the application field of hemp protein isolate (HPI), ultrasonic treatment and HPI were introduced to improve the properties of SPI emulsion gel and to explore the mechanism. The results showed that the gel strength (218.6 g) and water-holding capacity (86.24 %) of the emulsion gels were improved under ultrasonic treatments when the ratio of SPI:HPI was >6:4, and the reticulation structure of the gels was enhanced. When the ratio of SPI:HPI was <6:4, the gel structure was loose and formless. Ultrasonic treatment has a significant effect on the emulsion gel with the ratio of SPI:HPI was >6:4. Appropriate ultrasonic treatment (400 W) changed the protein structure, improved the rheological properties of emulsion gels to form the protein-oil-coated network structure. However, excessive ultrasonic treatment (600 W) will destroy the conformation of the protein, reducing the stability of the structure. The effect of ultrasonic treatment on emulsion gels with the ratio of SPI:HPI was <6:4 is low, but improved the gel protein digestibility. This study provides a theoretical basis for the application of ultrasonic in composite protein emulsion gels systems and the development and application of HPI., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

The study elucidates that the pH shifting treatment unfolds the conformation of soybean protein isolate (SPI), enabling it to intertwine with bacterial cellulose (BC) and form SPI/BC co-assemblies. Results from intrinsic fluorescence spectroscopy and surface hydrophobicity indicate that the SPI with pH shifting treatment shows a notable blue shift in maximum emission wavelength and increased surface hydrophobicity. It demonstrates that pH shifting treatment facilitates the unfolding of SPI's molecular conformation, promoting its entanglement with high aspect ratio BC. Particle size distribution and microstructural analysis further demonstrate that the pH shifting treatment facilitates the formation of SPI/BC co-assemblies. Evaluation of processing properties reveals that the SPI/BC co-assemblies exhibited exceptional gel and emulsification properties, with gel strength and emulsifying activity respectively six and two times higher than natural SPI. This enhancement is attributed to the thickening properties of BC with a high aspect ratio and the superior hydrophobicity of SPI in its molten globule state., Competing Interests: Declaration of competing interest The authors declared that they have no conflicts of interest to this work. We declare that we do not have any commercial or associative interest that represents a conflict of interest in connection with the work submitted., (Copyright © 2024. Published by Elsevier Ltd.)

Soybean protein isolate-soluble soybean polysaccharide (SPI-SSPS) complexes and mixtures with varying SPI/SSPS concentration ratios (1: 1, 2:1, 4:1, 8:1) were prepared by Maillard reaction and blending, respectively, and their physicochemical, structure, and functional properties were compared studied. The physical stability of SPI-SSPS complex, which consisted of CN and CS bonds, was better than that of the SPI/SSPS mixture with electrostatic interactions and hydrogen bonds, and both were superior SPI alone. The complex with SPI/SSPS concentration ratio of 8:1 had the highest grafting degree (33.25 %) and a more ordered structure, making its solubility and emulsifying property lower than the SPI/SSPS mixture; however, the physical and thermal stability of the SPI-SSPS complex was higher than that of the SPI and SPI/SSPS mixture. In particular, the SPI-SSPS complex with a high grafting degree showed a higher thermal denaturation temperature (194.06 °C). This study aimed to provide effective modification methods to utilize soybean processing by-products by modifying soybean protein isolate with soluble soybean polysaccharide., Competing Interests: Declaration of competing interest The authors declare no conflict of interest., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Plant protein's gelation is crucial in various food applications, and hydrolysis may enhance their gelation properties. In this study, we prepared soybean protein isolate hydrolysates (SPIH) using trypsin and/or papain, and found significant improvement in the solubility and gelling properties. These proteases broken down the peptide bonds and caused the exposure of hydrophobic groups as well as the unfolding of protein. Low molecular weight (<35 kDa) SPIHs were generated by the two-step enzymatic hydrolysis, showing significant improvements in storage modulus (G'), loss modulus (G″), viscosity, strength, and water-holding capacity (WHC). Among, PT-10 exhibited the highest WHC (61.72 ± 0.36 %), gel strength (4.67 ± 0.12 g), and network cross-linking density (0.33 ± 0.01 mol/m 3 ), while its solubility was also significantly increased up to 254 %. According to the results of gel molecular force interactions, disulfide bonds, hydrophobic interactions and hydrogen bonds involved in the gel network formation. These findings reveal that the appropriate hydrolysis modification may improve SPI gel's properties and expand its application in gel foods., Competing Interests: Declaration of competing interest The authors declare that they have no competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

A novel nanocomplex was prepared using soybean protein isolate (SPI) and oxidized fucoidan (OFU) to explore the structural and interaction variations and evaluate its potential for quercetin delivery. The optimized SPI to OFU mass ratio of 10:1 (SFU3) resulted in a nanocomplex particle size of 198.1 nm and increased ζ-potential. The incorporation of OFU altered the structure of SPI with the decrease in α-helix and β-sheet, and the redshift and intensity drop in fluorescence spectra. X-ray photoelectron spectroscopy (XPS) confirmed the Schiff base reaction between the two, interacting through covalent imine bonds. Moreover, OFU improved the micromorphology, antioxidant capacity, and stability of Quercetin (Que) nanocomplexes, with SFU3 showing the highest encapsulation efficiency and loading amount (94.80 %, 16.96 μg/mg). The nanocomplexes achieved an effective controlled release of Que. in vitro simulated digestion. This study will provide important insights into the development of SPI-OFU as nutrient carriers., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

In this study, the effects of faba bean protein concentrate (FPC) and soy protein isolate (SPI) on the microstructure and texture of high-moisture meat analogs (HMMA) were extensively analyzed using rheological methodologies. Rheological analyses revealed that introducing FPC disrupted the gel structure and hindered the formation of a protein network among the SPIs. The gel stability also indicated that higher FPC content increased the susceptibility to continuous oscillation, potentially resulting in structural collapse. The β-sheets content decreased from 43.55 % to 37.19 % as the FPC content increased. The observed decline in the textural properties of HMMA, accompanied by microstructural alterations and diminished protein alignment, further supported the hypothesis that FPC disrupts protein network formation. Additionally, as the FPC content increased, the content of disulfide bonds decreased, emphasizing the role of FPC as a texture modulator that affects the rubbery texture of SPI., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Plasticizer and thermal denaturation are indeed important factors for soybean protein film formation. The objective of the study was to investigate the effects of glycerol and thermal denaturation on the film-forming performances of soybean protein isolate (SPI) and elucidate the underlying mechanisms. From the results, glycerol had almost no effect on the protein's secondary and tertiary structures. Indeed, the dispersion of glycerol diminished the intra- or intermolecular hydrogen bonding of SPI and interacted with the amino acids of subunits through hydrogen bonding and van der Waals forces. By interfering with protein network interactions, the glycerol molecule achieved a plasticizing effect on SPI films. The effects of heat treatment on SPI film properties were mainly realized through the changes in molecular conformation caused by protein denaturation, which manifested in the enhancement of light barrier and mechanical capabilities, and markedly altered the distribution of water states within the film network. This study provided valuable insights to clarify the mechanism of protein film formation., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The current study investigated valorization of lignin nanoparticles (LNPs) and phenolic compounds loaded in chitosan (DLECNPs) extracted from date palm leaves into the soy protein isolate (SPI) biocomposite films. The mechanical, structural, barrier, physiochemical, thermal, optical, antioxidant, and antimicrobial properties of the formulated composite films were investigated. The findings showed that the incorporation of DLECNPs into the SPI films significantly improved the film's antioxidant properties by more than 3 times and showed antibacterial inhibition zone in the range of 10-15 mm against six pathogenic bacteria. Further, incorporating LNPs into SPI-DLECNPs films notably improved the mechanical properties from 4.32 MPa and 29.27 % tensile strength and elongation at break, respectively to 10.13 MPa and 54.94 %, the water vapor permeability from 7.38 g/Pa s m to 5.59 g/Pa s m, and the antibacterial inhibition zone from a range of 10.2 mm to 15.0-21.5 mm as well as making the films more heterogeneous and stronger than control SPI film. Moreover, LNPs changed the initial films' color from light yellow to dark red and reduced the films' transparency. The results indicated that LNPs reinforced SPI composite films showed significant improvements in several properties and thus can be used as a potential ingredient for formulation of biodegradable packaging films., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal conflict of interest that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)

In this experiment, the co-constructed O/W emulsions of different soy protein hydrolysates (SPHs) and gum arabic (GA) were investigated. SPHs were prepared by hydrolyzing soy protein isolate (SPI) using different enzymes, and investigated the effects of enzyme types and hydrolysis time on the physicochemical properties of SPHs. Moreover, SPI/GA and SPHs/GA were prepared and used as hydrophilic emulsifiers to construct O/W emulsions. The results showed that the optimal hydrolysis times for bromelain, pepsin and trypsin were 2 h (BSPH2), 3 h (PSPH3) and 3 h (TSPH3), respectively. Compared with SPI/GA emulsions, SPHs/GA emulsions had smaller particle size, more negative charge, higher interfacial adsorbed protein, and more stable emulsion systems. During the digestion process, SPHs/GA emulsions were effective in realizing the release of bioactives. In conclusion, enzymatic hydrolysis can be an effective modification technique, and SPHs/GA can be used as an effective emulsifier for the emulsion system., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

An increased interest has been observed in the application of soybean protein isolate (SPI) into O/W emulsion because of the amphipathic characteristics of SPI. However, at pH around 4.5, SPI was almost lost its hydrophilic characteristic, thus greatly limiting its application in emulsion under an acidic environment. Therefore, this drawback of SPI needs to be urgently solved. This study aims to investigate the effect of γ-polyglutamic acid (γ-PGA) on physicochemical properties of SPI-stabilized O/W emulsion. The results suggested that the interaction between γ-PGA and SPI improved the SPI solubility in solution, and increased emulsifying properties of SPI in the pH range of 4.0-5.0 via electrostatic interaction. Meanwhile, the charge neutralisation between SPI emulsions with γ-PGA was confirmed via ζ-potentiometry. With the presence of γ-PGA in emulsion at pH 4.0 and 5.0, the electrostatic complexation between SPI and anionic γ-PGA exhibited decreased the viscosity of SPI emulsion, which might be related to the phenomenon as indicated by the confocal laser scanning microscope measurements. Therefore, the electrostatic complexation between SPI and γ-PGA suggested that the promising potential of γ-PGA to be used in SPI-stabilized O/W emulsion under an acidic environment., Competing Interests: DECLARATION OF CONFLICTING INTERESTSThe author(s) declared no potential conflicts of interest with respect to the research, authorship, and/or publication of this article.

The study aimed to evaluate a food adhesive developed using tea polyphenols (TPs) with soybean protein isolate (SPI) to create a cohesive bond between soy protein gel and simulated fat. Upon the addition of 5.0 % TPs, significant increases in viscosity, thermal stability, and crystallinity were noted in adhesives, suggesting the formation of a cohesive network. Furthermore, TPs effectively enhanced adhesion strength, with the optimal addition being 5.0 %. This enhancement can be attributed to hydrogen bonding, hydrophobic and electrostatic interactions between TPs and SPI molecules. TPs induced a greater expansion of the protein structure, exposing numerous buried hydrophobic groups to a more hydrophilic and polar environment. However, excessive TPs were found to diminish adhesion strength. This can be attributed to enhanced reactions between TPs and SPI, where high molecular weight SPI-TPs cooperatively aggregate to form agglomerates that eventually precipitated, rendering the adhesive network inhomogeneous, less stable, and more prone to disruption., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The interaction mechanism between soybean protein isolate (SPI) and furan flavor compounds with different structures is studied using spectroscopy, molecular docking, and MD simulation methods. The order of binding ability between SPI and furan flavor compounds is 2-acetylfuran>furfural>5-methylfurfural. The structural differences (position and quantity of methyl groups) of three furan flavor compounds are key factors leading to the different adsorption abilities of SPI for furan flavor compounds. The findings from spectroscopy analyses suggest that the interaction between SPI and furan flavor compounds involves both static and dynamic quenching mechanisms, with static quenching being the main factor. Molecular docking and MD simulations reveal the atomic-level mechanisms underlying the stable binding for SPI and furan flavor compounds at spatiotemporal multiscale. This study provides a theoretical framework for the production and adjustment of meat essence formula in the production of soybean protein-based meat products., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

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., Competing Interests: Declaration of competing interest The authors declare no conflict of interest., (Copyright © 2023. Published by Elsevier Ltd.)

Soybean protein isolate (SPI) is widely used in the food industry. However, SPI-based emulsion gels tend to aggregate and undergo oiling-off during freeze-thawing. In this study, emulsion gels were prepared by a combination of heat treatment and ionic cross-linking using SPI and sodium alginate (SA) as raw materials. The focus was on exploring the mechanistic effects of the SPI-SA double network structure on the freeze-thaw stability of emulsion gels. The results showed that the addition of SA could form different types of network structures with SPI, due to different degrees of phase separation. In addition, SA appearing on the SPI network indicated that the addition of Ca 2+ shielded the electrostatic repulsion between SPI and SA to form SPI-SA complexes. The disappearance of the characteristic peaks of SA and SPI in Fourier transform infrared spectroscopy analysis also confirmed this view. Low-field nuclear magnetic resonance data revealed that SA played a role in restricting water migration within the emulsion gels, increasing bound water content, and thereby improving the water-holding capacity of the emulsion gels. Therefore, the incorporation of SA improved the freeze-thaw stability of SPI emulsion gels. These findings offer a theoretical basis and technical support for SPI application in frozen products., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

This study examined the impacts of ultrasonic power (0, 150, 300, 450, 600, and 750 W) and ultrasonic durations (3, 6, 9, 12, and 15 min) on the physicochemical properties and microstructure of diacylglycerol (DAG)-loaded emulsions stabilized with soybean protein isolate (SPI) and sodium alginate (SA). The findings indicated that the smallest particle size, zeta potential, and contact angle for SPI-SA-DAG emulsions were respectively 5.58 μm, -49.85 mV, and 48.65°, achieved at an ultrasonic power of 450 W. The emulsification properties, loss modulus, storage modulus, and apparent viscosity of the emulsions were optimal at this power setting and at a duration of 9 min. Analytical techniques, including confocal laser scanning-, scanning electron-, and atomic force microscopy, revealed that ultrasonication significantly altered emulsion aggregation state, with the surface roughness (Rq) being minimized at 450 W. These results demonstrated that the stability of SPI-SA-DAG emulsions can be effectively enhanced by an appropriate ultrasonic treatment at 450 W for 9 min. This research provides theoretical support for the broad application of sonication techniques in the food industry., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Author(s). Published by Elsevier B.V. All rights reserved.)

The non-covalent and covalent complexes of ultrasound treated soybean protein isolate (SPI) and soybean isoflavone (SI) were prepared, and the structure, physicochemical properties and in vitro digestion characteristics of SPI-SI complexes were investigated. Ultrasonic treatment increased the non-covalent and covalent binding degree of SPI with SI, and the 240 W ultrasonic covalent complexes had higher binding efficiency. Appropriate ultrasonic treatment caused more uniform particle size distribution, lower average particle size and higher surface charge, which enhanced the free sulfhydryl groups and surface hydrophobicity, thus improving the stability, solubility and emulsifying properties of complexes. Ultrasonic treatment resulted in more disordered secondary structure, tighter tertiary conformation, higher thermal stability and stronger SPI-SI covalent interactions of complexes. These structural modifications of particles had important effects on the chemical stability and gastrointestinal digestion fate of SI. The ultrasonic covalent complexation had a greater resistance to heat-induced chemical degradation of SI and improved its chemical stability. Furthermore, the 240 W ultrasonic covalent complexes showed lower protein digestibility during digestion, and provided stronger protection for SI, which improved the digestion stability and antioxidant activity. Therefore, appropriate ultrasound promoted SPI-SI interactions to improve the stability and functional properties of complexes, which provided a theoretical basis for the development of new complexes and their applications in functional foods., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

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)., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)

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., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This study is focused on exploring the effect of twin-screw high-moisture extrusion technology on the physico-chemical properties of β-glucan-soybean protein isolate (SPI-BG) extrudates. Different proportions (0 %, 1 %, 2 %, 3 %, 4 %, 5 %) of oat β-glucan (BG) were added with soybean protein isolate (SPI) to prepare SPI-BG extrudates. Results showed that the addition of a high quantity of β-glucan (BG) decreased the elastic properties of soy protein isolate (SPI) extrudates and then increased. The strengthening of S1-S2-S3 interactions (hydrogen bonds, hydrophobic interactions, and disulfide bonds) was primarily responsible for this trend. Fourier transform infrared (FTIR) spectral analysis was conducted which revealed that BG did not significant affect random coil content of SPI. However, it was observed that α-helix content was increased significantly and the β-sheet content was decreased. An observation was noted in the value of enthalpy (ΔH) change that increased from 115.80 J/g to 159.68 J/g., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)

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., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Author(s). Published by Elsevier B.V. All rights reserved.)

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 × 10 6  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., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Background: Metal ions commonly inevitably appear in food products and have adverse effects on high-internal-phase emulsions (HIPEs) foods, but conformational conversion of soybean protein isolate (SPI)/soybean soluble polysaccharide (SSPS) on the interface layer of HIPEs influenced by different metal ions has rarely been reported., Results: Here, the conformational conversion of SPI/SSPS induced by Na + , K + , Ca 2+ , Mg 2+ and Fe 3+ ions and its effects on HIPEs were investigated. After adding the ions to SPI and SPI/SSPS dispersions, the particle size and zeta potential results showed different degrees of flocculation; the zeta potential and Fourier transform infrared spectra indicated that SPI and SPI/SSPS changes in structure involve electrostatic interactions and hydrogen bonding. Moreover, Raman spectra showed that the content of β-sheet of SPI/SSPS HIPEs increased with the addition of Ca 2+ , Mg 2+ and Fe 3+ , suggesting that SPI molecules at the interface formed a more orderly structure. The ultraviolet and fluorescence results showed that the hydrophobic environment of tryptophan and tyrosine residues inside protein molecules played a vital role in the emulsifying stability of SPI., Conclusion: These findings suggested that the SPI/SSPS complexes for food applications were not susceptible to ions, thus ensuring complex stability, showing potential for commercial application in the production of emulsions. © 2023 Society of Chemical Industry., (© 2023 Society of Chemical Industry.)

The formation of a single soybean protein isolate (SPI) gel is limited by the processing conditions, and has the disadvantages of poor gel property, and it is usually necessary to add other biomacromolecules to improve its property. In this study, we investigated the effects of polysaccharide concentration on gel properties and interaction mechanisms of Tremella fuciformis polysaccharide (TFP)-SPI complexes. It was found that (1) the rheological properties, texture properties, water-holding properties, and thermal stability of TFP-SPI composite gels were improved with the addition of TFP (0.25-2.0 %, w/v) in a concentration-dependent manner; (2) hydrogen bond, the electrostatic interaction, hydrophobic interaction, and disulfide bond in the gel system increased with the increase of TFP concentration; (3) the electrostatic and hydrophobic interactions played an important role in the formation of the TFP-SPI composite gel while hydrogen bond formation was the least contributor to the binary composite gel network. Overall, TFP is not only a critical health food but also a promising structural component for improving the gel properties of SPI., Competing Interests: Declaration of competing interest Yuting Tian reports financial support was provided by National Natural Science Foundation of China., (Copyright © 2024 Elsevier B.V. All rights reserved.)

In this investigation, soybean protein isolate-rutin (SPI-RT) complexes were treated using dynamic high-pressure microfluidization (DHPM). The effects of this process on the physicochemical and thermodynamic properties of SPI were investigated at different pressures. Fourier-transform infrared spectroscopy and fluorescence spectroscopy provided evidence that the SPI structure had been altered. The binding of SPI to RT resulted in a decrease in the percentage of α-helices and random curls as well as an increase in the percentage of β-sheets. In particular, the α-helix content decreased from 29.84 % to 26.46 %, the random curl content decreased from 17.45 % to 15.57 %, and the β-sheet content increased from 25.37 % to 26.53 %. Moreover, fluorescence intensity decreased, and the emission peak of the complex was red-shifted by 6 nm, exposing the internal groups. Based on fluorescence quenching analysis, optimal SPI-RT complexation was achieved after 120-MPa DHPM treatment, and molecular docking analysis verified the interaction between SPI and RT. The minimum particle size, maximum absolute potential, and total phenolic content of the complexes were 78.06 nm, 21.4 mV and 74.35 nmol/mg protein, respectively. Furthermore, laser confocal microscopy revealed that the complex particles had the best microstructure. Non-covalent interactions between the two were confirmed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Moreover, the hydrophobicity of the complex particle's surface increased to 16,045 after 120-MPa DHPM treatment. The results of this study suggest that DHPM strongly promotes the improvement of the physicochemical properties of SPI, and provide a theoretical groundwork for further research., Competing Interests: Declaration of competing interest The authors declared that they have no conflicts of interests in this manuscript., (Copyright © 2024 Elsevier B.V. All rights reserved.)

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 m 2 /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., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)

Multifunctional mulch films with robust mechanical behaviors of biopolymer-based biodegradable mulch materials were highly demanded in promoting the development of "green" agriculture. Herein, a sort of mechanically robust and all-biodegradable soybean protein isolate-graft‑sodium carboxymethyl cellulose composite mulch film was innovatively proposed through the amidation reactions between -COOH on protonated sodium carboxymethyl cellulose and -NH 2 on soybean protein isolate. Arising from the reinforced intermolecular interactions upon chemical covalent bonds and physical hydrogen bonds, the maximum tensile strength and the elongation at break were increased from 10.61 MPa and 20.67 % for sodium carboxymethyl cellulose film to 42.15 MPa and 24.8 % for the optimized soybean protein isolate-graft‑sodium carboxymethyl cellulose composite mulch film, respectively. In addition, experimental results showed that the optimized soybean protein isolate-graft‑sodium carboxymethyl cellulose composite mulch film possesses soil moisture retention and controlled urea release properties. When employed as mulch film in practice, the cabbage seed presents higher germination when soil was covered with this versatile mulch film compared to commercial low-density polyethylene mulch film. Our discoveries build a prototype for the manufacture of eco-friendly mulch films with high mechanical strength, soil moisture retention, controlled urea release features., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)

The elderly people are prone to dysphagia due to weakened muscle strength. 3D food printing could modify the nutritional ratio and shape design to produce personalized nutritious food suitable for patients with dysphagia. White mushroom (Agaricus bisporus) is rich in a variety of active ingredients such as polysaccharides and polyphenols which are beneficial to human body, but its unique texture is not suitable for patients with dysphagia to chew. This study investigated the impact of different concentrations of soybean protein isolate (SPI, 3%, 5%, 7%, w/w) on 3D food printing of white mushroom powder and carried out the hierarchical representation of dysphagia diet within the framework of International Dysphagia Diet Standardization Initiative (IDDSI). The results illustrated that SPI addition to white mushroom gel reduced water mobility and promoted hydrogen bond formation, which significantly improved the mechanical strength and cohesiveness of printing inks, including yield stress, viscosity and hardness. IDDSI tests showed that the SPI addition of 3% and 5% helped the printing ink pass the spoon tilt test and the fork drip test, which could be classified as level 5 minced and moist food under the consideration of the fork pressure test. The 3D printing results indicated that the 7% SPI addition made the yield stress too high and was not easy for extrusion, resulting in the appearance defects of the printed sample. The addition of 3% SPI could make the printed sample have smooth surface and excellent self-supporting capacity. This work provides insights of white mushroom 3D printing technology as a more visually appealing dysphagia diet., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)

This study aimed to investigate the effects of different wheat bran arabinoxylan (WBAX) concentrations (1, 2, 3, and 4 wt%) on the structural and physicochemical properties of WBAX-soybean protein isolate (SPI) emulsion-filled gels (EFGs) prepared using laccase and heat treatment. The properties of the various gels as well as their microstructure, rheology, and in vitro digestion behaviors were investigated. Results showed that WBAX-SPI EFGs with a 3 wt% WBAX concentration had a smooth and uniform appearance, high water holding capacity (98.5 ± 0.2 %), and enhanced mechanical properties. Rheological experiments suggested that a stronger and closer gel network was formed at 3 wt% WBAX concentration. Fourier transform infrared spectroscopy showed that laccase and heat treatment not only catalyzed the intramolecular crosslinking of WBAX and SPI, respectively, but also promoted the interaction between WBAX and SPI. Confocal laser scanning microscopy revealed that the WBAX gel network was interspersed within the SPI network. The interactions contributing to the gelation analysis revealed that chemical (disulfide bond) and physical (hydrogen bond and hydrophobic) interactions promoted the formation of denser EFGs. Furthermore, the WBAX-SPI EFGs provided a β-carotene bioaccessibility of 21.8 ± 0.6 %. Therefore, our study suggests that WBAX-SPI EFGs hold promising potential for industrial applications in the delivery of β-carotene., Competing Interests: Declaration of competing interest The authors declare no known competing financial interests., (Copyright © 2023 Elsevier B.V. All rights reserved.)

To identify the ideal soybean protein isolate for texturized vegetable protein processing, the effect of different soybean protein isolates on texturized vegetable protein composition was studied. Three different types of soybean protein isolates were selected and analyzed for functional properties (water holding capacity (WHC), emulsifying properties, foaming properties), amino acid content, and protein secondary structure. Then, using the same formulation, the soybean protein isolates were extruded to produce texturized vegetable protein, and its textural properties, degree of texturization, microstructure, free sulfhydryl (free SH), and disulfide (S-S) content were determined. Lastly, a correlation analysis was performed to examine the connection between soybean protein isolates and texturized vegetable proteins. After correlation analysis, the soybean protein isolate functional properties that affect the textural properties of the texturized vegetable protein were as follows: the emulsifying property affected the hardness, adhesiveness, springiness, gumminess, and chewiness of the texturized vegetable proteins; and the foaming property affected the gumminess, chewiness, and the degree of texturization of the texturized vegetable proteins. In addition, 16 amino acids including threonine (Thr), methionine (Met), and arginine (Arg) affect texturized vegetable proteins, mainly with respect to adhesiveness, springiness, and free SH. The effects of secondary structure (α-helix, random coil) on texturized vegetable proteins were degree of texturization, resilience, and cohesion, respectively. Therefore, choosing the soybean protein isolate with better emulsifying and foaming properties provides a more suitable approach for processing texturized vegetable protein.

To improve the stability of the soybean protein isolate/chitosan/sodium alginate ternary complex coacervate phase against environmental pH and ionic strength, the complex ternary phase cross-linked by Ca 2+ was characterized and evaluated. The viscoelastic properties, thermal properties, microstructure, and texture profile were characterized using rheology, differentia scanning calorimetry as well as thermmogravimetric analysis, scanning electron microscopy as well as transmission electron microscopy, and texture profile analysis, respectively. Compared with the uncross-linked ternary complex coacervate, the complex in situ cross-linked with 1.0 % Ca 2+ for 1 h still retains its typical solid characteristics, and has a more compact network structure and better stability. Our research results also showed that prolonging the cross-linking time (from 3 h to 5 h) and increasing the concentration of the cross-linking agent (from 1.5 % to 2.0 %) did not further improve the rheological, thermodynamic and textural properties of the complex coacervate. The ternary complex coacervate phase cross-linked in situ under 1.5 % concentration of Ca 2+ for 3 h showed significantly improved stability at low pH 1.5-3.0, which indicats that the ternary complex coacervate phase cross-linked in situ by Ca 2+ can be used as a potential delivery platform for the effective delivery of biomolecules under physiological conditions., Competing Interests: Declaration of competing interest We declare that there is no conflict of interest., (Copyright © 2023. Published by Elsevier B.V.)

A soybean protein isolate (SPI)-apricot polysaccharide gel with hypolipidemic activity that can be used for 3D printing was prepared and the mechanism of its gel formation was studied in this work. The results demonstrated that adding apricot polysaccharide to SPI could effectively improve the bound water content, viscoelastic properties and rheological properties of the gels. Low-field NMR, FT-IR spectroscopy and surface hydrophobicity confirmed that the interactions between SPI and apricot polysaccharide were mainly realized by electrostatic interactions, hydrophobic and hydrogen bonding. Furthermore, adding modified polysaccharide treated by ultrasonic-assisted Fenton method to SPI on the basis of low-concentration apricot polysaccharide contributed to improving the 3D printing accuracy and stability of the gel. Consequently, the gel formed by adding apricot polysaccharide (0.5 %, m/v) and modified polysaccharide (0.1 %, m/v) to SPI had the best hypolipidemic activity (the binding rate of sodium taurocholate and sodium glycocholate were 75.33 % and 72.86 %, respectively) and 3D printing characteristics., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier B.V. All rights reserved.)

The effects of heating temperature on epitopes, IgE-binding capacity, and conformation of soybean protein isolate (SPI) were investigated in this study. Indirect ELISA demonstrated that the IgE binding capacity of SPI was increased by 13.1 %-31.6 % after being heated at 60-100 °C for 20 min. SDS-PAGE demonstrated no changes in protein profiles, and native PAGE revealed the formation of aggregates. Structural analyses demonstrated the protein unfolding, appearing temperature-dependent, thus exposing conformational epitopes. Peptide mapping analysis revealed the changes in peptide profiles of major allergens (Gly m 4, Gly m 5, Gly m 6, P28, and Kunitz trypsin inhibitor). LC/MS-MS demonstrated that heating caused the masking or exposure of linear epitopes in Gly m 4 - Gly m 6 and P28. Therefore, heating caused structural changes to expose epitopes to increase IgE binding capacity in SPI. Patients with soybean allergy should avoid the heated SPI until the results of clinical trials are confirmed., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

Spatial structure and amino acid residue side-chain oxidative modification of soybean isolated protein (SPI) at different dry heating temperatures (70, 100, 130, 160 and 190 °C) were investigated, respectively in this study. The results showed that the dry heating promoted the formation of disulfide bonds and oxidative modification of SPI, such as carboxylation and hydroxylation under the below 160 °C. With increasing temperature, β-sheet and α-helix shifted to random coil and β-turn. The conformation of SPI changed, the solubility decreased and the particle size became smaller resulting from the combination of protein oxidation and chemical bond redistribution, but the structural integrity of SPI was better ensured below 130 °C. SPI was severely hydrolyzed at 190 °C. These results provide a theoretical basis for the study of protein modification by dry heating, which is a guideline for controlling the degree of protein denaturation in the food industry., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

A suitable carrier for flax lignans using Soybean protein isolated (SPI) - κ-carrageenan (KC) hydrogels was developed. The effects of KC concentration on the stability of hydrogels were investigated, as well as water holding capacity (WHC), syneresis and morphological changes. A solid-like gel network and viscoelasticity of composite hydrogels were confirmed by rheological behavior test. Scanning electron microscopy (SEM) displayed a dense and uniform structure for hydrogels with the optimum KC concentration (0.6 %). Fourier Transform Infrared Spectroscopy (FTIR) and Differential Scanning Calorimetry (DSC) curves suggested lignan might interact with SPI and KC by hydrogen bonding or hydrophobic effects. The release of flax lignans in hydrogels was followed with Fick diffusion in simulated gastric fluids (SGF) and non-Fickian diffusion in simulated intestinal fluids (SIF), respectively. The cumulative release rate of flax lignan in complex gels (46.00 %) was lower than that of pure SPI hydrogels (77.43 %) at the end of digestion. The results indicated that KC protected the protein by hindering the accession of digestive enzymes into the hydrogels, thus resulting in a reduction of gel matrix erosion and lignan release during digestion. These findings shield a light on SPI-KC hydrogels as carriers for water-soluble bioactive compounds in food and pharmaceutical industries., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier B.V. All rights reserved.)

Backgrounds: In the present study, a glycosylated soybean protein with glucose was prepared after pH treatment under different conditions (5.0, 6.0 7.0, 8.0, 9.0) and the conformation and emulsifying properties of soybean protein isolate (SPI) and soybean protein isolate-glucose (SPI-G) were investigated., Results: The degree of grafting (37.11%) and browning (39.2%) of SPI-G conjugates were obtained at pH 9.0 (P < 0.05). The results of analysis of polyacrylamide gel electrophoresis, Fourier transform infrared spectroscopy and Endogenous fluorescence spectroscopy showed that the Maillard reaction between the SPI and glucose occurred and the natural rigid structure of test proteins was stretched and became looser, and thus the tertiary conformation was unfolding. Furthermore, the particle size of the all of samples was reduced under different pH conditions, indicating that pH treatment can increase the flexibility of SPI molecules. The proteins exhibited the best surface hydrophobicity, thermal stability and emulsifying activity (EA) of modified products when subjected to a pH treatment of 9.0, whereas they afforded the best emulsion stability (ES) at pH 8.0. There was a good correlation between the molecular flexibility and emulsifying properties of SPI-G [0.963 (F:EA) and 0.879 (F:ES)] (P < 0.05)., Conclusion: The present study shows that the structural and emulsification characteristics of natural SPI and SPI-G conjugates have been significantly enhanced via pH treatment and these results provide a theoretical guidance for the application of glycosylated SPI in the food industry. © 2022 Society of Chemical Industry., (© 2022 Society of Chemical Industry.)

Soybean protein isolate (SPI)-dextran conjugate-based nanogels were prepared via the Maillard reaction combined with protein self-assembly in this study. The dextran molecular weight (40 kDa), SPI/dextran mass ratio (1:1.75), and incubation time (3.3 d) for preparing SPI-dextran conjugate (SDC) were firstly optimized. The SDC was confirmed by analyzing the changes in protein composition and infrared absorption bands and showed loosened tertiary conformation, reduced surface hydrophobicity, decreased Z-average hydrodynamic diameter (D h ) and zeta potential, and improved emulsifying properties compared to the native SPI. Effects of conjugate concentration, pH, heating temperature, and time on D h and polydispersity index were also evaluated. The SDC-based nanogels were translucent in aqueous solution and exhibited a spherical core-shell structure with a D h of ∼104.4 nm and a good stability against thermal treatment, ionic strength, and storage. Results demonstrated the SDC-based nanogels possessed a potential to be used as desirable nanocarriers for encapsulating hydrophobic bioactive compounds., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

In this study, citrus pectin (CP) and soybean protein isolate (SPI) were used as raw materials to prepare a complex. The interaction mechanism and structural changes between SPI and CP were deeply studied by fluorescence spectroscopy and Fourier infrared spectroscopy. The results show that CP has a strong quenching effect on SPI's endogenous fluorescence, and with the addition of CP, the endogenous fluorescence intensity of SPI decreased from 13,565.2 to 6067.3. The CP quenching of SPI is static quenching, and the number of combined bits is 1.26. The results of three-dimensional fluorescence spectra showed that the addition of CP reduced the polarity of SPI amino acid residue microenvironment and changed the protein structure. Hydrophobic interaction exists between CP and SPI. The results of three-dimensional fluorescence spectra showed that the addition of CP reduced the polarity of the amino acid residue microenvironment of SPI and changed the protein structure. Fourier transform infrared spectroscopy shows that CP could change the secondary structure of SPI by decreasing the α-helix and β-sheet, increasing β-rotation and irregular curl, destroying the ordered structure of SPI and increasing the polarity of the amino acids exposed to the solution. The microstructure analysis shows that SPI-CP composite system has honeycomb structure and dense pores. From the perspective of reaction thermodynamics, it was found that the addition of CP could improve the thermal stability of SPI and increase the denaturation temperature of SPI from 119.73 to 132.97°C. This study can provide a theoretical basis for the preparation of protein-pectin complexes and provides reference for their application in food grade gels and Pickering emulsions., (© 2022 Institute of Food Technologists®.)

Soybean proteins are the main component of plant-based meat alternatives in the Chinese market. The effects of non-covalent interactions between polyphenols and proteins on the protein structures, the rest physicochemical properties, and formations of heterocyclic amines (HAs) were examined using a polyphenols-containing soybean protein isolate (SPI) complex as a model to dry heating at 170℃ for 10 min. The results showed that tetrahydro-curcumin had extensive inhibitory effects on the HA formation. In addition, tea polyphenols, grapeseed procyanidins, and dihydromyricetin were also found to have inhibitory effects only on some HAs. Correlation analysis showed that polyphenols altered the secondary structure and steric structure of the protein by interacting with the protein, which affects the HA formation. The results provided theoretical references and a basis for the formation mechanisms of HAs in polyphenol-inhibiting protein foods., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

Background: The properties and stability of emulsion rely greatly on the emulsification method and emulsifier. In this study, different emulsification methods (high-speed homogenization, ultrasonic treatment and their combination) were employed for the preparation of emulsions stabilized by soybean protein isolate (SPI) and soy lecithin (SLT) at three ratios. The microstructure, hydrodynamic average diameter, ζ-potential, creaming stability and low-field nuclear magnetic resonance relaxation behaviors of emulsions were investigated., Results: The results indicated that the influence of emulsification method was closely related to the ratio of SPI/SLT. Overall, the SPI-SLT-stabilized emulsion treated by ultrasound showed better stability and uniformity, while the combined treatment of high-speed homogenization and ultrasound was helpful in improving the uniformity and stability of SPI-stabilized Pickering emulsion. However, the SLT-stabilized emulsions all exhibited worse uniformity in terms of particle size distribution and polydispersity index., Conclusion: These results will be helpful for selecting an appropriate emulsification method and emulsifier to improve the stability of emulsions. © 2021 Society of Chemical Industry., (© 2021 Society of Chemical Industry.)

Curcumin (Cur) is a natural polyphenol with beneficial biological and pharmacological activities; however, it has limited applications owing to its low solubility and light sensitivity. The protein-polysaccharide complex can effectively embed lipid-soluble drugs to increase their stability and dispensability in aqueous solutions. Soybean protein isolate (Spi) and fucoidan (Fuc) were used as a polymer matrix, and core-shell nanoparticles were prepared to encapsulate Cur via electrostatic interaction under acidic and neutral conditions. The structure of the Spi-Fuc nanoparticles was studied via Fourier-transform infrared spectroscopy, transmission electron microscopy, and scanning electron microscopy. Concurrently, we evaluated the efficacy of the nanoparticles based on stability, drug loading rate, and simulated release. Our results showed that the Spi-Fuc nanoparticles (size, approximately 236.56 nm) had a spherical, core-shell structure and that they could effectively load Cur with an embedding efficiency of >95%; moreover, the system had long-term dispersion stability. Thus, we provide a simple method for Cur delivery, which can also be potentially used for delivering lipid-soluble active ingredients., (Copyright © 2020 Elsevier B.V. All rights reserved.)

Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI dispersions were subjected to ACP treatments at different frequencies (80 to 100 Hz) and durations (1 to 10 min) to investigate the effects of exposing conditions. Results showed that ACP induced reactive oxygen species-mediated oxidation of soy proteins, resulting in modifications in the secondary and ternary structures of SPI. As a consequence, functional properties of SPI, such as emulsifying (56 to 168%, compared with control) and foaming properties (60 to 194%) were influenced by varying degrees. In addition, under certain circumstance (120 Hz, 5 min), the IgE-binding level of SPI was decreased by up to 75%, when compared to the control. Moderate treatment yielded products with improved functionality and reduced allergenicity, while extensive exposure induced a loss of vendibility due to protein aggregation. PRACTICAL APPLICATION: In this study, we demonstrated for the first time, that plasma species reacted with soybean proteins, resulting in spatial structural changes which are closely related with protein functionality and allergenicity. ACP interacts with macromolecules in aqueous systems and thus can be an alternative and promising nonthermal approach in modifying soybean proteins, whereas the exact role of different processing parameters needs to be well-elaborated., (© 2020 Institute of Food Technologists®.)

Soybean protein isolate (SPI) was incubated with flaxseed gum (FG) at 60 °C for 3 days under high hydrostatic pressure (HHP 0.1-300 MPa). Results showed improvement in solubility of SPI upon glycation with FG. The maximum solubility reached 86.84% when SPI-FG was treated at pH 8.0 and 200 MPa. The occurrence, degrees and sites of SPI-FG glycation suggested that moderate pressure (100 MPa) significantly promoted Maillard reactions, but higher pressures (greater than 200 MPa) suppressed these reactions. The secondary structure of the glycated proteins varied greatly with respect to α-helix and random coil contents and vibrations of the amide II band at 200 MPa. These microstructural changes increased the solubility over a broad pH range. The conformational changes in the glycated SPI supported the improved solubility of SPI-FG. Overall, HHP represents a potential method of controlling glycation to improve protein processability and expand their applicability in the food industry., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2020 Elsevier Ltd. All rights reserved.)

Soybean protein isolate (SPI) powders were prepared at different ultrafine grinding time, and the functional and flavor properties of microparticulation SPI were evaluated. With extending ultrafine grinding time, a narrow and uniform particle size distribution in SPI powders was produced. The particle sizes of protein powders at grinding time 0, 2, 4, 6 and 8 h significantly reduced from 217 ± 16.5-137.5 ± 10.7 nm, while the absolute values of zeta-potential significantly increased from 25 ± 0.93-32.4 ± 117 mV (P < 0.05). The microstructure of SPI at grinding time 0-8 h changed from smooth to irregular. With prolonging the ultrafine grinding processing time, the solubility, foaming and emulsifying properties of SPI powders were improved, the content ofα-helix, β-sheet and random coils increased, while β-turn decreased. Furthermore, the ultrafine grinding time clearly influenced the volatile compounds of SPI powders. The main flavor compounds were aldehydes, alcohols, acids, ketones and alkanes. SPI powders for grinding time 2, 4, 6 and 8 h exhibited the higher total content of volatile compounds compared to that for 0 h. So the ultrafine grinding treatment at appropriate time could affect the functional and flavor properties of SPI., (Copyright © 2020 Elsevier B.V. All rights reserved.)

Effects of a novel slit divergent ultrasound (SDU) treatment on soybean protein isolate (SPI)-lentinan conjugates via Maillard reaction was investigated. Besides, the stability of emulsions prepared by SPI and SPI-lentinan conjugates (ultrasound and un-ultrasound) as emulsifiers was compared. The results showed that ultrasonic treatment (40 min) markedly increased the degree of grafting (26.48%) by 1.91 times comparing with traditional heating method (2 h, 13.89%). In addition, structural analysis showed that the conjugates obtained by SDU treatment changed the secondary structure and had higher surface hydrophobicity and fluorescence intensity than those obtained by traditional heating method. Apart from this, SDU treatment could significantly improve the functional properties (solubility, foaming, emulsifying capacity, thermal stability, and viscosity) of conjugates. Furthermore, the emulsions prepared by the SPI-lentinan conjugates (ultrasound) as emulsifiers possessed the highest stability against environmental stresses. Taken together, SDU-assisted heating could be an excellent method to improve the functional properties of conjugates., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2020 Elsevier Ltd. All rights reserved.)

The effects of native starch (NS), acetylated starch (AS), and acetylated distarch phosphate (ADSP) on the gel properties of soybean protein thermal gel were investigated using texture analysis, low-field nuclear magnetic resonance (LF-NMR) spectroscopy, dynamic rheometry and scanning electron microscopy. The results of the textural profile analysis showed that 10% ADSP increased the hardness and chewiness of the mixed gel, while NS and AS led to decreases in the textural properties. The results of the LF-NMR analysis indicated that the AS improved the water-holding capacity of the mixed gel due to the transformation of weakly bound water to strongly bound water. During heating and cooling, the rheological profiles of the elastic (G') and viscous modulus (G″) of all the samples exhibited a two-stage pattern of decrease and then increase, and the final values of G' and G″ reached maxima when the ADSP content was 10%. The scanning electron microscopy images showed that the ADSP granules dispersed in the gel network. The integrity of the starch granules was crucial for regulating the properties of the soybean protein gel. These results provided information about the further design and preparation of soybean protein foods containing modified starch., (Copyright © 2019 Elsevier B.V. All rights reserved.)

In this work, a facile approach was developed to synthesized alcalase-inorganic hybrid nanocomposite (alcalase@CaHPO 4 ) by immobilizing alcalase with calcium hydrogen phosphate (CaHPO 4 ). The nanocomposite possessed flower-like morphological features with excellent hydrolysis activity on soybean protein isolates (SPI) with 1.57 fold higher compared to free alcalase. The experiment was evident of alcalase@CaHPO 4 hybrid nanoflowers with 90% sustainability after the seven cycles of reusability and 80-100% relative activity at 50-70 °C and with 65% at pH 4 in acidic condition. Soybean protein hydrolysates (SPHs) produced by immobilized alcalase possessed 70% radical-scavenging capacity at 0.8 mg/mL concentration and 20% calcium-binding capacity at pH 6. The solubility of SPHs produced by alcalase@CaHPO 4 hybrid nanoflowers was also improved by 15% compared to free alcalase. The high radical scavenging capability, good calcium binding capacity and improved solubility of SPHs prepared through alcalase@CaHPO 4 hybrid nanoflowers would be highly promising in food industries., (Copyright © 2019 Elsevier Ltd. All rights reserved.)