TY - JOUR
T1 - Peptidases and amino acid catabolism in lactic acid bacteria
AU - Christensen, Jeffrey E.
AU - Dudley, Edward G.
AU - Pederson, Jeffrey A.
AU - Steele, James L.
N1 - Funding Information:
The authors would like to thank our colleagues Jeff Broadbent and Carmen Peláez for communicating results prior to publication. The work on peptidases and amino acid catabolism conducted in our laboratory was supported in part by the College of Agricultural and Life Sciences at the University of Wisconsin-Madison and the Center for Dairy Research through funding from Dairy Management Inc.
PY - 1999
Y1 - 1999
N2 - The conversion of peptides to free amino acids and their subsequent utilization is a central metabolic activity in prokaryotes. At least 16 peptidases from lactic acid bacteria (LAB) have been characterized biochemically and/or genetically. Among LAB, the peptidase systems of Lactobacillus helveticus and Lactococcus lactis have been examined in greatest detail. While there are homologous enzymes common to both systems, significant differences exist in the peptidase complement of these organisms. The characterization of single and multiple peptidase mutants indicate that these strains generally exhibit reduced specific growth rates in milk compared to the parental strains. LAB can also catabolize amino acids produced by peptide hydrolysis. While the catabolism of amino acids such as Arg, Thr, and His is well understood, few other amino acid catabolic pathways from lactic acid bacteria have been characterized in significant detail. Increasing research attention is being directed toward elucidating these pathways as well as characterizing their physiological and industrial significance.
AB - The conversion of peptides to free amino acids and their subsequent utilization is a central metabolic activity in prokaryotes. At least 16 peptidases from lactic acid bacteria (LAB) have been characterized biochemically and/or genetically. Among LAB, the peptidase systems of Lactobacillus helveticus and Lactococcus lactis have been examined in greatest detail. While there are homologous enzymes common to both systems, significant differences exist in the peptidase complement of these organisms. The characterization of single and multiple peptidase mutants indicate that these strains generally exhibit reduced specific growth rates in milk compared to the parental strains. LAB can also catabolize amino acids produced by peptide hydrolysis. While the catabolism of amino acids such as Arg, Thr, and His is well understood, few other amino acid catabolic pathways from lactic acid bacteria have been characterized in significant detail. Increasing research attention is being directed toward elucidating these pathways as well as characterizing their physiological and industrial significance.
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U2 - 10.1023/A:1002001919720
DO - 10.1023/A:1002001919720
M3 - Article
C2 - 10532381
AN - SCOPUS:0032872645
SN - 0003-6072
VL - 76
SP - 217
EP - 246
JO - Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology
JF - Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology
IS - 1-4
ER -