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[胰凝乳蛋白酶水解乳蛋白的初始动力学]

[Initial kinetics of milk protein hydrolysis by chymotrypsin].

作者信息

Vorob'ev M M, Levicheva I Iu, Belikov V M

出版信息

Prikl Biokhim Mikrobiol. 1996 Mar-Apr;32(2):237-41.

PMID:8725446
Abstract

The kinetics of the initial stages of hydrolysis of alpha- and beta-caseins, alpha-lactalbumin, beta-lactoglobulin, and bovine serum albumin was studied quantitatively by electrophoresis. The hydrolysis rates of caseins (demasked polypeptide chains) exceeded the rates of the degradation of milk whey proteins limited by the protein globule demasking by more than two orders of magnitude. Even relatively accessible for hydrolysis globular proteins (beta-lactoglobulin and BSA) were hydrolyzed by the one-by-one mechanism. The maximum value of the ratio between the rates of the peptide chain demasking and the protein globule hydrolysis was 0.0035.

摘要

通过电泳对α-和β-酪蛋白、α-乳白蛋白、β-乳球蛋白以及牛血清白蛋白水解初始阶段的动力学进行了定量研究。酪蛋白(去掩蔽的多肽链)的水解速率比受蛋白质球去掩蔽限制的乳清蛋白降解速率高出两个多数量级。即使是相对易于水解的球状蛋白(β-乳球蛋白和牛血清白蛋白)也是通过逐个机制进行水解的。肽链去掩蔽速率与蛋白质球水解速率之间的最大比值为0.0035。

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