Hydrolysis of casein-derived peptides αS1-casein(f1-9) and β-casein(f193-209) by Lactobacillus helveticus peptidase deletion mutants indicates the presence of a previously undetected endopeptidase

被引：16

作者：

Christensen, JE

Broadbent, JR

Steele, JL ^{[1
]}

机构：

[1] Univ Wisconsin, Dept Food Sci, Madison, WI 53706 USA

[2] Univ Wisconsin, Dept Bacteriol, Madison, WI 53706 USA

[3] Utah State Univ, Dept Nutr & Food Sci, Logan, UT 84322 USA

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 2003年 / 69卷 / 02期

关键词：

D O I：

10.1128/AEM.69.2.1283-1286.2003

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Peptides derived from hydrolysis of alpha(s1)-casein(fl-9) [alpha(s1)-CN(fl-9)] and beta-CN(f193-209) with cell extracts of Lactobacillus helveticus CNRZ32 and single-peptidase mutants (DeltapepC, DeltapepE, DeltapepN, DeltapepO, and DeltapepX) were isolated by using reverse-phase high-performance liquid chromatography and were characterized by mass spectrometry. The peptides identified suggest that there was activity of an endopeptidase, distinct from previously identified endopeptidases (PepE and PepO), with specificity for peptide bonds C terminal to Pro residues. Identification of hydrolysis products derived from a carboxyl-blocked form of beta-CN(f193-209) confirmed that the peptides were derived from the activity of an endopeptidase.

引用

页码：1283 / 1286

页数：4

共 23 条

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