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 Microbioljournal_title
Applied and environmental microbiologyauthors
Chen YS,Steele JLdoi
10.1128/AEM.64.9.3411-3415.1998subject
Has Abstractpub_date
1998-09-01 00:00:00pages
3411-5issue
9eissn
0099-2240issn
1098-5336journal_volume
64pub_type
杂志文章abstract::The ability of Streptococcus species to selectively adhere to the oral epithelial cells of newborns was studied in vitro. On day 1 of life, mucosal cells from normal infants demonstrated selective attraction for the natural distribution of streptococci that would soon colonize these surfaces. Streptococcus salivarius ...
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journal_title:Applied and environmental microbiology
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