地衣芽孢杆菌蛋白酶活性产生的乳清蛋白水解物的聚集特性。

Aggregation properties of whey protein hydrolysates generated with Bacillus licheniformis proteinase activities.

作者信息

Spellman David, Kenny Patricia, O'Cuinn Gerard, FitzGerald Richard J

机构信息

Department of Life Sciences, University of Limerick, Ireland.

出版信息

J Agric Food Chem. 2005 Feb 23;53(4):1258-65. doi: 10.1021/jf048754a.

DOI:10.1021/jf048754a

PMID:15713050

Abstract

Hydrolysis of whey protein concentrate (WPC) with Alcalase 2.4 L, a Bacillus licheniformis proteinase preparation, induces gelation. The aggregation behavior of WPC hydrolysates generated with Alcalase and Prolyve 1000, a Bacillus licheniformis proteinase that did not induce gelation, were studied by turbidity and particle size analysis. With the use of synthetic peptide substrates, it was shown that Alcalase contains a glutamyl endopeptidase (GE) activity not present in Prolyve. Comparison of the aggregation behavior of WPC hydrolysates generated with Alcalase, Prolyve, and combinations of Prolyve with a GE activity isolated from Alcalase showed that GE was responsible for the observed enzyme-induced peptide aggregation in Alcalase hydrolysates. Hydrolysates generated with Prolyve, having a degree of hydrolysis (DH) of 11.8% and 10.4% of peptide material greater than 10 kDa, could be induced to aggregate by the addition of GE. These results emphasize the contribution of enzyme specificity to the physicochemical and functional characteristics of proteinase hydrolysates of WPC.

摘要

用芽孢杆菌蛋白酶制剂地衣芽孢杆菌蛋白酶2.4L水解乳清浓缩蛋白（WPC）会诱导凝胶化。通过浊度和粒度分析研究了用碱性蛋白酶和Prolyve 1000（一种不会诱导凝胶化的地衣芽孢杆菌蛋白酶）产生的WPC水解产物的聚集行为。通过使用合成肽底物，发现碱性蛋白酶含有Prolyve中不存在的谷氨酰胺内肽酶（GE）活性。比较用碱性蛋白酶、Prolyve以及Prolyve与从碱性蛋白酶中分离出的GE活性的组合产生的WPC水解产物的聚集行为，表明GE是碱性蛋白酶水解产物中观察到的酶诱导肽聚集的原因。用Prolyve产生的水解产物，水解度（DH）为11.8%，大于10 kDa的肽物质占10.4%，通过添加GE可诱导聚集。这些结果强调了酶特异性对WPC蛋白酶水解产物的物理化学和功能特性的贡献。