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Genetic Characterization and Physiological Role of Endopeptidase O from Lactobacillus helveticus CNRZ32

Genetic Characterization and Physiological Role of Endopeptidase O from Lactobacillus helveticus... Genetic Characterization and Physiological Role of Endopeptidase O from Lactobacillus helveticus CNRZ32 Yo-Shen Chen and James L. Steele * Department of Food Science, University of Wisconsin—Madison, Madison, Wisconsin 53706 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied and Environmental Microbiology American Society For Microbiology

Genetic Characterization and Physiological Role of Endopeptidase O from Lactobacillus helveticus CNRZ32

Genetic Characterization and Physiological Role of Endopeptidase O from Lactobacillus helveticus CNRZ32

Applied and Environmental Microbiology , Volume 64 (9): 3411 – Sep 1, 1998

Abstract

Genetic Characterization and Physiological Role of Endopeptidase O from Lactobacillus helveticus CNRZ32 Yo-Shen Chen and James L. Steele * Department of Food Science, University of Wisconsin—Madison, Madison, Wisconsin 53706 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.

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Publisher
American Society For Microbiology
Copyright
Copyright © 1998 by the American society for Microbiology.
ISSN
0099-2240
eISSN
1098-5336
Publisher site
See Article on Publisher Site

Abstract

Genetic Characterization and Physiological Role of Endopeptidase O from Lactobacillus helveticus CNRZ32 Yo-Shen Chen and James L. Steele * Department of Food Science, University of Wisconsin—Madison, Madison, Wisconsin 53706 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

Applied and Environmental MicrobiologyAmerican Society For Microbiology

Published: Sep 1, 1998

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