Effect of pH-shifting treatment on the structural and functional properties of soybean protein isolate and its interactions with (–)-epigallocatechin-3-gallate

Yan, Shizhang; Xu, Jingwen; Zhang, Xiaoying; Xie, Fang; Zhang, Shuang; Jiang, Lianzhou; Qi, Baokun; Yang, Linzhang

doi:10.1016/j.procbio.2020.10.016

Cited by 88 publications

(29 citation statements)

References 43 publications

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“…The free sulfhydryl group concentration is an important parameter that affects the protein interface and emulsification behavior, the difference in which could reflect the effect of EDTAD acylation treatment on the covalent interactions of protein 6 . More hydrophobic residues could be exposed on the surface of the SPI, which would lead to the enhancement of surface hydrophobicity H 0 33 . The higher the surface hydrophobicity, the higher the degree of unfolding in the protein molecule.…”

Section: Resultsmentioning

confidence: 99%

Study on preparation of acylated soy protein and stability of emulsion

Xia

Zheng

et al. 2021

J Sci Food Agric

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BACKGROUND Protein can be used as an emulsifier to improve emulsion stability at the interface of water‐in‐oil emulsion. However, natural soybean protein isolate (SPI) does not meet the high demands as an emulsifier in the food industry. The effect of acylation modification by ethylenediaminetetraacetic dianhydride (EDTAD; 0–300 g kg−1) on the physicochemical properties of SPI was studied. RESULTS The results of the Fourier transform infrared spectra analyses showed that carboxyl groups were introduced into the SPI structure by the EDTAD treatment. The carboxyl concentration of SPI was increased by 30–74.07% with an increase in EDTAD addition from 50 to 300 g kg−1. When 150 g kg−1 EDTAD was added, the surface hydrophobicity, the emulsifying activity, and the absolute value of the zeta potential were increased by 213%, 120%, and 68% respectively, and the particle size decreased to 247 nm. The droplet size of emulsion decreased to 10 μm when pH was 6. At the same concentration of SPI and pH, the absolute value of zeta potential of the emulsion was biggest. A comparison of the emulsions during storage showed the improvement of emulsion stability was related to the increase in the zeta potential and the decrease in the average particle size. The experimental group showed no destabilization on day 21, and no obvious aggregation phenomenon was observed. CONCLUSION Acylation modification by EDTAD changed the emulsifying properties of SPI and enhanced the stability of the SPI emulsion. © 2021 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 99%

Study on preparation of acylated soy protein and stability of emulsion

Xia

Zheng

et al. 2021

J Sci Food Agric

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“…The dynamic quenching constant ( K SV ) and static quenching constant ( K q ) were calculated based on the Stern–Volmer equation. For static quenching reactions, the binding constant ( K A ) and the number of binding sites ( n ) can be calculated as follows 16 :

\frac{F_{0}}{F} goodbreak= 1 goodbreak+ K_{SV} ([], Q) goodbreak= 1 goodbreak+ K_{q} τ_{0} ([], Q)

\lg ((), \frac{F_{0} - F}{F}) goodbreak= \lg K_{A} goodbreak+ italicnlg ([], Q)

where F 0 and F are the fluorescence intensity of the sample solution in the absence and the presence of the quencher, respectively; [Q] is the concentration of GA (mol L −1 ), K SV and K q are the dynamic quenching constant (L mol −1 ) and static quenching constant (L/mol•s), respectively, and τ 0 is the average lifetime of the fluorophore in the absence of the quencher (s).…”

Section: Methodsmentioning

confidence: 99%

“…The dynamic quenching constant (K SV ) and static quenching constant (K q ) were calculated based on the Stern-Volmer equation. For static quenching reactions, the binding constant (K A ) and the number of binding sites (n) can be calculated as follows 16 :…”

Section: Characterization Of Complexes Fluorescence Quenching Mechani...mentioning

confidence: 99%

Effect of enzymatic hydrolysis conditions on structure of soy protein isolate/gum arabic complex and stability of oil‐in‐water emulsion

et al. 2022

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BACKGROUND The emulsifying, antioxidant and foaming properties of soy protein isolate hydrolysates (SPH) can be improved by the addition of gum arabic (GA). We investigated the effects of different hydrolysis conditions on the complexation of SPH and GA, and the effects of the complex on the properties of emulsions. RESULTS Fluorescence spectroscopy showed that the addition of GA had a stronger effect on bromelain and pepsin hydrolysates than trypsin hydrolysate, and therefore had a higher binding constant (KA) and a larger number of binding sites (n). The addition of GA could also improve protein solubility and emulsifying ability. The emulsions prepared with complexes, especially the complex of GA and SPH obtained by pepsin hydrolysis for 3 h, had a high absolute charge value, uniform particle size distribution, stable morphology, and good storage stability. After storage, the emulsification index (CI) of the emulsion only increased to 23.08%; its 1,1‐diphenyl‐2‐picrylhydrazyl (DPPH) free radical scavenging activity was 24.37 ± 1.22% and its 2,2'‐Azinobis‐(3‐ethylbenzthiazoline‐6‐sulphonate) (ABTS+) free radical scavenging activity was largely retained. CONCLUSION During long‐term storage, pepsin‐treated protein (especially protein treated for 3 h) and GA can form a stable emulsion with antioxidant properties. This work provides new ideas for the development of natural and safe emulsifiers that have antioxidant properties and can be stored long‐term and used in the food industry. © 2022 Society of Chemical Industry

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“…Using a Schrödinger Sitemap, four binding pockets were obtained on soybean 11S glycinin. To evaluate the accessibility of four pockets, molecular docking was carried out using epigallocatechin gallate (EGCG), a known SPI binder [3,19], as the ligand. As shown in Figure 1, EGCG was docked into the four pockets individually.…”

Section: Binding-pocket Identification and Egcg Dockingmentioning

confidence: 99%

Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies

Liu

et al. 2021

Foods

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(1) Background: Protein–polyphenol interactions have been widely studied regarding their influence on the properties of both protein and the ligands. As an important protein material in the food industry, soybean protein isolate (SPI) experiences interesting changes through polyphenols binding. (2) Methods: In this study, a molecular docking and virtual screening method was established to evaluate the SPI–polyphenol interaction. A compound library composed of 33 commonly found food source polyphenols was used in virtual screening. The binding capacity of top-ranking polyphenols (rutin, procyanidin, cyanidin chloride, quercetin) was validated and compared by fluorescence assays. (3) Results: Four out of five top-ranking polyphenols in virtual screening were flavonoids, while phenolic acids exhibit low binding capacity. Hydrogen bonding and hydrophobic interactions were found to be dominant interactions involved in soybean protein–polyphenol binding. Cyanidin chloride exhibited the highest apparent binding constant (Ka), which was followed by quercetin, procyanidin, and rutin. Unlike others, procyanidin addition perturbed a red shift of SPI fluorescence, indicating a slight conformational change of SPI. (4) Conclusions: These results suggest that the pattern of SPI–polyphenol interaction is highly dependent on the detailed structure of polyphenols, which have important implications in uncovering the binding mechanism of SPI–polyphenol interaction.

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Effect of pH-shifting treatment on the structural and functional properties of soybean protein isolate and its interactions with (–)-epigallocatechin-3-gallate

Cited by 88 publications

References 43 publications

Study on preparation of acylated soy protein and stability of emulsion

Study on preparation of acylated soy protein and stability of emulsion

Effect of enzymatic hydrolysis conditions on structure of soy protein isolate/gum arabic complex and stability of oil‐in‐water emulsion

Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies

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