Hydrolysis of casein-derived peptides alpha(S1)-casein(f1-9) and beta-casein(f193-209) by Lactobacillus helveticus peptidase deletion mutants indicates the presence of a previously undetected endopeptidase.
Peptides derived from hydrolysis of alpha(S1)-casein(f1-9) [alpha(S1)-CN(f1-9)] and beta-CN(f193-209) with cell extracts of Lactobacillus helveticus CNRZ32 and single-peptidase mutants (Delta pepC, Delta pepE, Delta pepN, Delta pepO, and Delta 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 beta-CN(f193-209) confirmed that the peptides were derived from the activity of an endopeptidase.
Christensen
Jeffrey E
JE
Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Broadbent
Jeffery R
JR
Steele
James L
JL
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D002364:Caseins / Q000737:chemistry / Q000378:metabolism*; D003470:Culture Media; D010450:Endopeptidases / Q000378:metabolism; D017353:Gene Deletion; D006868:Hydrolysis; D007778:Lactobacillus / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000235:genetics* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*
D000596:Amino Acids; D002364:Caseins; D003470:Culture Media; D010455:Peptides; D010450:Endopeptidases; D010447:Peptide Hydrolases