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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Effect of Enzymatic Deamidation on the Heat-induced Conformational Changes in Whey Protein Isolate and Its Relation to Gel Properties
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Effect of Enzymatic Deamidation on the Heat-induced Conformational Changes in Whey Protein Isolate and Its Relation to Gel Properties

机译：酶脱酰胺作用对乳清蛋白分离物热诱导构象变化的影响及其与凝胶性质的关系

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摘要

The effect of proteih-glutamiriase (PG) on the heat-induced conformational changes in whey protein isolate (WPI) and its relation to gel properties was investigated. The structural properties of WPI treated with PG were examined by several analytical methods. The analysis of the fluorescence spectrum and the binding capacity of a fluorescent probe demonstrated that deamidation prevented the increase in the fluorescence intensity caused by subsequent heat treatment. Measurements of the molecular weight distribution of WPI showed that PG-treated WPI was not likely to polymerize even after heating. This is thought to be due to an increase in electrostatic repulsion between carboxylic acid groups and a decrease in the formation of disulfide bonds, which results in the decrease in heat-induced aggregation. The properties of heat-induced WPI gels were modified by deamidation. PG-treated WPI gels had a soft texture and a high water-holding capacity in the presence of salts.
机译：研究了蛋白谷氨酰胺酶（PG）对乳清蛋白分离物（WPI）中热诱导的构象变化的影响及其与凝胶性质的关系。用几种分析方法检查了用PG处理的WPI的结构性能。荧光光谱和荧光探针的结合能力的分析表明，脱酰胺作用防止了由随后的热处理引起的荧光强度的增加。 WPI分子量分布的测量表明，即使在加热后，PG处理的WPI也不太可能聚合。认为这是由于羧酸基团之间的静电斥力增加和二硫键形成的减少所致，这导致热诱导的聚集减少。热诱导的WPI凝胶的特性通过脱酰胺改性。 PG处理的WPI凝胶在盐存在下具有柔软的质地和高保水能力。

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