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Applied and Environmental Microbiology, February 2003, p. 1283-1286, Vol. 69, No. 2
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.2.1283-1286.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Hydrolysis of Casein-Derived Peptides _S1-Casein(f1-9) and ß-Casein(f193-209) by Lactobacillus helveticus Peptidase Deletion Mutants Indicates the Presence of a Previously Undetected Endopeptidase

Jeffrey E. Christensen,^1, Jeffery R. Broadbent,² and James L. Steele^3*

Department of Bacteriology,¹ Department of Food Science, University of Wisconsin-Madison, Madison, Wisconsin 53706,³ Department of Nutrition and Food Sciences, Utah State University, Logan, Utah 84322²

Received 8 April 2002/ Accepted 1 November 2002

Peptides derived from hydrolysis of _S1-casein(f1-9) [_S1-CN(f1-9)] and ß-CN(f193-209) with cell extracts of Lactobacillus helveticus CNRZ32 and single-peptidase mutants (pepC, pepE, pepN, pepO, and pepX) 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 ß-CN(f193-209) confirmed that the peptides were derived from the activity of an endopeptidase.

Present address: Clinical Research Department, Marshfield Medical Research Foundation, Marshfield, WI 54449.

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