Title

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

Document Type

Article

Journal/Book Title/Conference

Applied and Environmental Microbiology

Volume

69

Issue

2

Publisher

American Society of Microbiology

Publication Date

2003

First Page

1283

Last Page

1286

DOI

10.1128/AEM.69.2.1283-1286.2003

Abstract

Peptides derived from hydrolysis of αS1-casein(f1-9) [αS1-CN(f1-9)] and β-CN(f193-209) with cell extracts of Lactobacillus helveticus CNRZ32 and single-peptidase mutants (ΔpepC, ΔpepE, ΔpepN, ΔpepO, and ΔpepX) 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 β-CN(f193-209) confirmed that the peptides were derived from the activity of an endopeptidase.

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