Effects of proteolysis and transglutaminase crosslinking on physicochemical characteristics of walnut protein isolate

文献类型： 外文期刊

第一作者： Shi, Ai-Min

作者： Shi, Ai-Min;Jiao, Bo;Liu, Hong-Zhi;Zhu, Song;Shen, Min-jiang;Feng, Xiao-Long;Hu, Hui;Liu, Li;Faisal, Shah;Wang, Qiang;Adhikari, Benu

作者机构：

关键词： Enzymatic hydrolysis; Protein solubility; Morphology; Rheology

期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：4.952； 五年影响因子：5.383 ）

ISSN： 0023-6438

年卷期： 2018 年 97 卷

页码：

收录情况： SCI

摘要： In order to improve the functional properties of walnut protein isolate (WPI), the effect of partial hydrolysis with trypsin, crosslinking with transglutaminase (TGase), and combinations of both treatments on the physicochemical characteristics of WPI was investigated. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicated that WPI could be easily digested into smaller peptides by trypsin and could also be crosslinked into aggregates with high molecular weight. Hydrolyzing crosslinked WPI significantly increased its solubility from 9.73% to 54.54%. Scanning electron microscopy indicated that treatment with trypsin or TGase alone had a notable effect whereas the mixture of enzyme and TGase had a relatively lower effect on the microstructure of WPI. Hydrolysis did not affect the sulthydryl (-SH) content while TGase crosslinking significantly reduced (-SH) content from 92.9 mu moL/g to 47.06 mu moL/g. Hydrolysis markedly increased the surface hydrophobicity (H-0), while crosslinking did not significantly change H-0. TGase treatment increased the viscosity of hydrolysates, but the viscosity of trypsin hydrolysates was not altered. Treatment of WPI with both TGase and trypsin showed the lowest initial G' and G" values due to the highest solubility. Thus, WPI with proteolysis and transglutaminase treatment has great potential for applications in the food industry.

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