Covalent modification of soy protein isolate by (−)‐epigallocatechin‐3‐gallate: effects on structural and emulsifying properties

Tao, Fei; He, Jiang; Chen, Wenwei; Zhang, Yongyong; Jia-rong, Pan; Jiang, Jiaxin; Zhang, Jia

doi:10.1002/jsfa.9114

Cited by 37 publications

(10 citation statements)

References 42 publications

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“…The particle size of the droplets was more than ten times smaller than that of the control group. These results are consistent with those of Tao et al ., 44 indicating that the EDTAD modification improved the emulsifying properties and stability of SPI.…”

Section: Resultssupporting

confidence: 93%

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: 93%

Study on preparation of acylated soy protein and stability of emulsion

Xia

Zheng

et al. 2021

J Sci Food Agric

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“…20,37,40,58 Surface hydrophobicity of phenolic-protein conjugates is determined by using a hydrophobic uorescence probe, 1-anilino-8naphthalene sulfonate (ANS). 65 Particle size characteristics of the conjugates can be analyzed by dynamic light scattering (DLS). The zeta potential is measured to study the charges of the conjugates based on their movements in an electrical eld.…”

Section: Differential Scanning Calorimetry (Dsc)mentioning

confidence: 99%

Recent advances in phenolic–protein conjugates: synthesis, characterization, biological activities and potential applications

et al. 2019

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“…7,8 Recently, epigallocatechin-3-gallate (a poly-phenolic compound from tea) was used to cross-link SPI, resulting in altered secondary structure and better emulsion stability. 9 Caseins are the richest protein fraction in milk, whereas caseinate is a widely used protein ingredient in the food industry.…”

Section: Introductionmentioning

confidence: 99%

“…Under the action of transglutaminase (TGase, EC 2.3.2.13), an acyltransferase widely used in past research, proteins are cross‐linked and thus have enhanced modulus and viscosity in their dispersions 7,8 . Recently, epigallocatechin‐3‐gallate (a poly‐phenolic compound from tea) was used to cross‐link SPI, resulting in altered secondary structure and better emulsion stability 9 …”

Section: Introductionmentioning

confidence: 99%

Property changes of caseinate in response to its dityrosine formation induced by horseradish peroxidase, glucose oxidase and d‐glucose

Chang

et al. 2020

J Sci Food Agric

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BACKGROUND: A ternary system containing horseradish peroxidase (HRP), glucose oxidase and D-glucose using one-or twostep treatment was evidently able to cross-link proteins via dityrosine formation and thus was assessed for its possible impact on several properties of a protein ingredient caseinate. RESULTS: HRP, glucose oxidase and D-glucose were used at 200 U, 6 U and 0.05 mmol g −1 protein to treat caseinate by one-and two-step methods, producing two cross-linked caseinates named CLCN-I and CLCN-II, respectively. In response to the conducted cross-linking, both CLCN-I and CLCN-II gained slightly reduced dispersibility at pH 5-10, enlarged hydrodynamic radius (particle size distribution, 266.37 and 258.33 versus 226.67 nm) and negative zeta-potential (−26.60 and −22.27 versus −14.30 mV) in dispersions, increased water-binding (3.70 and 3.09 versus 2.68 kg kg −1 protein), decreased oil-binding (1.75 and 2.74 versus 2.87 kg kg −1 protein) and emulsifying activity (76.2 and 82.3 versus 94.3 m 2 g −1 protein), increased emulsion stability (84.3% and 82.5% versus 78.6%), and enhanced thermal stability with lower mass loss (58.5% and 59.6% versus 64.3%) or higher decomposition temperatures (331.2°C and 328.7°C versus 327.6°C) upon heating at 105-450°C. In addition, CLCN-I and CLCN-II had decreased gelling temperatures and shortened gelling times when forming acid-induced gels, and the gels were endowed with increased values in four textural indices and finer microstructure. Moreover, CLCN-I with a higher cross-linking extent showed greater property changes than CLCN-II. CONCLUSION: This ternary system could be used in caseinate cross-linking to improve properties such as aggregation, emulsification, gelation and thermal stability.

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Covalent modification of soy protein isolate by (−)‐epigallocatechin‐3‐gallate: effects on structural and emulsifying properties

Abstract: The covalent modification by EGCG improved the emulsifying property of SPI. This study therefore provided an innovative approach for improving the emulsifying properties of proteins. © 2018 Society of Chemical Industry.

Cited by 37 publications

References 42 publications

Study on preparation of acylated soy protein and stability of emulsion

Study on preparation of acylated soy protein and stability of emulsion

Recent advances in phenolic–protein conjugates: synthesis, characterization, biological activities and potential applications

Property changes of caseinate in response to its dityrosine formation induced by horseradish peroxidase, glucose oxidase and d‐glucose

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