pH-induced conformational changes and interfacial dilatational rheology of soy protein isolated/soy hull polysaccharide complex and its effects on emulsion stabilization

Wang, Shengnan; Yang, Jinjie; Shao, Guoqiang; Liu, Jie; Yang, Ling; Li, Jun; Liu, He; Zhu, Danshi; Li, Yang; Jiang, Lianzhou

doi:10.1016/j.foodhyd.2020.106075

Cited by 101 publications

(50 citation statements)

References 43 publications

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“…7. When the pH of each emulsion was identical, a smaller droplet size with a more uniform droplet dispersion resulted in a more stable emulsion, which is consistent with the research results of Wang et al 16 . The untreated protein cannot form a stable emulsion system due to its large particle size.…”

Section: Resultssupporting

confidence: 90%

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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: Resultssupporting

confidence: 90%

“…A Zetasizer Nano ZS90 (Malvern Panalytical Ltd, Malvern, UK) was used to measure the particle size, polymer dispersity index, and zeta potential of SPI samples in potential and granularity modes at 25 °C. The samples were injected into a disposable polystyrene cuvette and measured at a fixed angle of 90° with an equilibrium time of 120 s 16 …”

Section: Methodsmentioning

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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“…Compared with SPI microparticles, the content of α-helix and random coils of SPI/SA microparticles were reduced, the content of β-sheets was increased, and the content of β-turns did not change significantly. These results indicated that the addition of SA changed the conformation of the protein, and promoted the transition from a disordered to an ordered structure [32]. In addition, the H 0 of SPI/SA microparticles was lower than that of the SPI microparticles because the hydrophobic interaction between SA and SPI reduced the formation of disordered structures [41].…”

Section: Ftir Spectra Analysismentioning

confidence: 94%

“…At pH 5.0-11.0, the ζ-potential of the SPI microparticles changed from positive to negative charge. As the pH continued to increase, the absolute value of the ζ-potential of the SPI microparticles increased, which was attributed to the increased ionization of the carboxyl groups of the protein [32]. By contrast to the SPI microparticles, the SPI/SA microparticles all demonstrated a negative ζ-potential.…”

Section: ζ-Potential Analysismentioning

confidence: 99%

“…At pH 5.0, the maximum fluorescence intensity decreased to the lowest. This might be due to hydrophobic-interaction-induced aggregation of the protein at a pH near the pI [32]. At a pH far away from the pI, the unfolding of the protein structure caused more Trp and Tyr residues to be exposed, so the maximum fluorescence intensity of the SPI microparticles increased [27].…”

Section: Fluorescence Spectra Analysismentioning

confidence: 99%

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Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties

Cao

Tong

Wang

et al. 2022

Foods

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The effects of sodium alginate (SA) and pH value on the formation, structural properties, microscopic morphology, and physicochemical properties of soybean protein isolate (SPI)/SA microparticles were investigated. The results of ζ-potential and free sulfhydryl (SH) content showed electrostatic interactions between SA and SPI, which promoted the conversion of free SH into disulfide bonds within the protein. The surface hydrophobicity, fluorescence spectra, and Fourier transform infrared spectroscopy data suggested that the secondary structure and microenvironment of the internal hydrophobic groups of the protein in the SPI/SA microparticles were changed. Compared with SPI microparticles, the surface of SPI/SA microparticles was smoother, the degree of collapse was reduced, and the thermal stability was improved. In addition, under the condition of pH 9.0, the average particle size of SPI/SA microparticles was only 15.92 ± 0.66 μm, and the distribution was uniform. Rheological tests indicated that SA significantly increased the apparent viscosity of SPI/SA microparticles at pH 9.0. The maximum protein solubility (67.32%), foaming ability (91.53 ± 1.12%), and emulsion activity (200.29 ± 3.38 m2/g) of SPI/SA microparticles occurred at pH 9.0. The application of SPI/SA microparticles as ingredients in high-protein foods is expected to be of great significance in the food industry.

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

Yin

Zhang

et al. 2023

J Sci Food Agric

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

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pH-induced conformational changes and interfacial dilatational rheology of soy protein isolated/soy hull polysaccharide complex and its effects on emulsion stabilization

Cited by 101 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

Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties

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

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