热诱导蛋清蛋白对酶水解敏感性的变化：一项动力学研究。

Heat-induced changes in the susceptibility of egg white proteins to enzymatic hydrolysis: a kinetic study.

作者信息

Van der Plancken Iesel, Van Remoortere Marijke, Indrawati Indrawati, Van Loey Ann, Hendrickx Marc E

机构信息

Laboratory of Food Technology, Department of Food and Microbial Technology, Faculty of Agricultural and Applied Biological Sciences, Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, B-3001 Heverlee, Belgium.

出版信息

J Agric Food Chem. 2003 Jun 18;51(13):3819-23. doi: 10.1021/jf026019y.

DOI:10.1021/jf026019y

PMID:12797749

Abstract

A kinetic study was conducted on the effect of heating in the temperature range of 50-92 degrees C, on the susceptibility of ovalbumin and albumen solutions to enzymatic hydrolysis by a mixture of trypsin and alpha-chymotrypsin at 37 degrees C and pH 8.0. Heat treatment resulted in an increase in degree of hydrolysis after 10 min of enzymatic reaction of both ovalbumin and albumen, as measured using the pH-stat method. The time-dependent change in the susceptibility to enzymatic hydrolysis after heat treatment was described by a fractional conversion model (based on an apparent first-order reaction kinetic model). Different end levels of degree of hydrolysis were obtained after heating for a long time at different temperatures, which suggests that the final degree of unfolding of the protein is temperature dependent.

摘要

进行了一项动力学研究，考察在50 - 92摄氏度温度范围内加热，对卵清蛋白和蛋清溶液在37摄氏度、pH值为8.0条件下被胰蛋白酶和α-糜蛋白酶混合物进行酶解的敏感性的影响。采用pH计法测定，热处理导致卵清蛋白和蛋清在酶促反应10分钟后的水解程度增加。热处理后酶解敏感性随时间的变化用分数转化率模型（基于表观一级反应动力学模型）来描述。在不同温度下长时间加热后得到了不同的水解程度终末水平，这表明蛋白质的最终展开程度取决于温度。