The sol-gel-sol transformation behavior of egg white proteins induced by alkali

被引:64
作者
Gao, Xuejing [1 ]
Yao, Yao [1 ]
Wu, Na [1 ]
Xu, Mingsheng [1 ]
Zhao, Yan [2 ]
Tu, Yonggang [1 ]
机构
[1] Jiangxi Agr Univ, Jiangxi Key Lab Nat Prod & Funct Food, Nanchang 330045, Jiangxi, Peoples R China
[2] Nanchang Univ, Engn Res Ctr Biomass Convers, Minist Educ, Nanchang 330047, Jiangxi, Peoples R China
基金
中国国家自然科学基金;
关键词
Egg white; Gelation; Alkali; Sol-gel-sol; Transformation behavior; PHYSICOCHEMICAL PROPERTIES; RHEOLOGICAL PROPERTIES; FOAMING PROPERTIES; HIGH-PRESSURE; AGGREGATION; GELATION; MICROSTRUCTURE; PEPTIDES; YOLK; MECHANISM;
D O I
10.1016/j.ijbiomac.2020.03.209
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In the current study, we found an interesting phenomenon that fresh egg white (EW) undergo the sol-gel-sol transition with alkali treatment. The transformation behavior at different alkalinity (1.5%, 2.0%, and 2.5%) was investigated. As the gel formed, the hardness, lightness, surface hydrophobicity and the total number of identified peptides increased, and then, remarkable reduction when the gel collapsed. Rheological behavior indicated that the viscosity varied with shear rate. Fourier transform infrared spectroscopy (FTIR) showed that beta-sheets gradually decreased as the alpha-helices increased during gel-sol transformation. The quantification of EW peptides analysis revealed that there was no dramatic correlation between the number of identified peptides and alkalinity. It was concluded that the sol-gel-sol transition was strongly dependent on alkali levels, moreover, high concentration promoted gel formation as well as liquefaction. The EW transformation behavior induced by alkali had a significant effect on protein aggregation and denaturation, and further changed physicochemical properties. (C) 2020 Elsevier B.V. All rights reserved.
引用
收藏
页码:588 / 597
页数:10
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