Effects of Protein Openning Mode on Enzymatic Cross-linking and Antigenicity of Whey Protein

被引：0

作者：

Yu X. ^{[1
]}

Liu C. ^{[1
]}

Zhao Y. ^{[1
]}

Xu X. ^{[1
]}

Liu Z. ^{[1
]}

Zhang Y. ^{[1
]}

机构：

[1] Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin

来源：

Journal of Chinese Institute of Food Science and Technology | 2020年 / 20卷 / 09期

关键词：

Antigenicity; Crosslinking by transglutaminase (TGase); Cysteine; Heat treatment; Whey protein;

D O I：

10.16429/j.1009-7848.2020.09.007

中图分类号：

学科分类号：

摘要：

In order to investigate the effects of protein opening methods on the antigenicity and enzymatic cross-linking of whey protein, heating or cysteine treatment was used to open the molecular structure of whey protein. The modified whey protein was subjected to transglutaminase (TGase) cross-linking, and the molecular weight of the modified cross-linked product and the direct TGase cross-linked product was analyzed by polyacrylamide gel electrophoresis (SDS-PAGE). The antigenicity of whey protein was determined by an indirect competitive enzyme-linked immunosorbent assay and the hydrophobicity of whey proteins and their modified products was determined. The experimental results showed that the intrinsic fluorescence and surface hydrophobicity of the heat-treated whey protein modified product were higher than the cysteine modified product. From the results of SDS-PAGE, it was found that the cysteine-modified whey protein were more than the cross-linked product obtained by heat modification. The results of antigenic analysis showed that the heat treatment reduced the antigen content in whey protein by about 20%, and the cysteine modification reduced the antigen content in whey protein by more than 30%. The results showed that cysteine modification could significantly reduce the antigenicity of whey protein more than heat treatment. © 2020, Editorial Office of Journal of CIFST. All right reserved.

引用

页码：53 / 58

页数：5

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