Genetic characterization and physiological role of endopeptidase O from Lactobacillus helveticus CNRZ32.

Abstract:

:A previously identified insert expressing an endopeptidase from a Lactobacillus helveticus CNRZ32 genomic library was characterized. Nucleotide sequence analysis revealed an open reading frame of 1,941 bp encoding a putative protein of 71.2 kDa which contained a zinc-protease motif. Protein homology searches revealed that this enzyme has 40% similarity with endopeptidase O (PepO) from Lactococcus lactis P8-2-47. Northern hybridization revealed that pepO is monocistronic and is expressed throughout the growth phase. CNRZ32 derivatives lacking PepO activity were constructed via gene replacement. Enzyme assays revealed that the PepO mutant had significantly reduced endopeptidase activity when compared to CNRZ32 with two of the three substrates examined. Growth studies indicated that PepO has no detectable effect on growth rate or acid production by Lactobacillus helveticus CNRZ32 in amino acid defined or skim milk medium.

journal_name

Appl Environ Microbiol

authors

Chen YS,Steele JL

doi

10.1128/AEM.64.9.3411-3415.1998

subject

Has Abstract

pub_date

1998-09-01 00:00:00

pages

3411-5

issue

9

eissn

0099-2240

issn

1098-5336

journal_volume

64

pub_type

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