The Effects of Ethanol and Rutin on the Structure and Gel Properties of Whey Protein Isolate and Related Mechanisms

被引：11

作者：

Jia, Na ^{[1
]}

Lin, Shiwen ^{[1
]}

Yu, Yuzhen ^{[1
]}

Zhang, Guangyao ^{[1
]}

Li, Lingli ^{[1
]}

Zheng, Duoduo ^{[1
]}

Liu, Dengyong ^{[1
]}

机构：

[1] Bohai Univ, Coll Food Sci & Technol, Natl & Local Joint Engn Res Ctr Storage, Jinzhou 121013, Peoples R China

来源：

FOODS | 2022年 / 11卷 / 21期

关键词：

whey protein isolate; rutin; ethanol; gel properties; interactions; BETA-LACTOGLOBULIN; PHYSICOCHEMICAL PROPERTIES; FUNCTIONAL-PROPERTIES; POLYPHENOLS; PH; DENATURATION; ULTRASOUND; CAPACITY; GELATION; BINDING;

D O I：

10.3390/foods11213480

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The effects of different levels of rutin (0, 0.05%, 0.1%, 0.2% and 0.3% w/v) and ethanol on the structure and gel properties of whey protein isolate (WPI) were examined. The results showed that the addition of ethanol promoted the gel formation of WPI. The addition of rutin increased the gel strength of WPI and maintained the water-holding capacity of the gel. Ethanol caused an increase in thiol content and surface hydrophobicity, but rutin decreased the thiol content and surface hydrophobicity of WPI. The particle size, viscosity and viscoelasticity of WPI increased at rutin levels of 0.2% and 0.3%, indicating that rutin caused cross-linking and aggregation of WPI, but rutin had no significant effect on the zeta-potential, indicating that electrostatic interactions were not the main force causing the changes in protein conformation and gel properties. Ethanol and rutin improved the gel properties of WPI possibly by inducing cross-linking of WPIs via hydrophobic and covalent interactions.

引用

页数：15

共 48 条

[21] Effect of Ethanol on the Textural Properties of Whey Protein and Egg White Protein Hydrogels during Water-Ethanol Solvent Exchange [J].