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酸性蛋白酶A和蛋白酶M对α-乳白蛋白的选择性水解作为胃蛋白酶替代方法的比较:乳清蛋白中β-乳球蛋白的纯化潜力

Comparison of selective hydrolysis of α-lactalbumin by acid Protease A and Protease M as alternative to pepsin: potential for β-lactoglobulin purification in whey proteins.

作者信息

Lisak Jakopović Katarina, Cheison Seronei Chelulei, Kulozik Ulrich, Božanić Rajka

机构信息

Laboratory for Technology of Milk and Milk products, Faculty of Food Technology and Biotechnology,University of Zagreb,Pierottijeva 6, HR-10000, Zagreb,Croatia.

Global Applied Science & Technology (GAST), Mars GmbH,Eitzerstr 215, D-27283 Verden (Aller),Germany.

出版信息

J Dairy Res. 2019 Feb;86(1):114-119. doi: 10.1017/S0022029919000086. Epub 2019 Feb 7.

DOI:10.1017/S0022029919000086
PMID:30729897
Abstract

The experiments reported in this research paper examine the potential of digestion using acidic enzymes Protease A and Protease M to selectively hydrolyse α-lactalbumin (α-La) whilst leaving β-lactoglobulin (β-Lg) relatively intact. Both enzymes were compared with pepsin hydrolysis since its selectivity to different whey proteins is known. Analysis of the hydrolysis environment showed that the pH and temperature play a significant role in determining the best conditions for achievement of hydrolysis, irrespective of which enzyme was used. Whey protein isolate (WPI) was hydrolysed using pepsin, Acid Protease A and Protease M by randomized hydrolysis conditions. Reversed-phase high performance liquid chromatography was used to analyse residual proteins. Regarding enzyme selectivity under various milieu conditions, all three enzymes showed similarities in the reaction progress and their potential for β-Lg isolation.

摘要

本研究论文中报道的实验考察了使用酸性酶蛋白酶A和蛋白酶M进行消化,以选择性水解α-乳白蛋白(α-La)同时使β-乳球蛋白(β-Lg)相对保持完整的潜力。将这两种酶与胃蛋白酶水解进行了比较,因为已知胃蛋白酶对不同乳清蛋白的选择性。水解环境分析表明,无论使用哪种酶,pH值和温度在确定实现水解的最佳条件方面都起着重要作用。通过随机水解条件,使用胃蛋白酶、酸性蛋白酶A和蛋白酶M对乳清蛋白分离物(WPI)进行水解。采用反相高效液相色谱法分析残留蛋白质。关于各种环境条件下的酶选择性,所有三种酶在反应进程及其分离β-Lg的潜力方面都表现出相似性。

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