Antonie van Leeuwenhoek

, Volume 76, Issue 1, pp 217–246

Peptidases and amino acid catabolism in lactic acid bacteria

  • Jeffrey E. Christensen
  • Edward G. Dudley
  • Jeffrey A. Pederson
  • James L. Steele
Article

DOI: 10.1023/A:1002001919720

Cite this article as:
Christensen, J.E., Dudley, E.G., Pederson, J.A. et al. Antonie Van Leeuwenhoek (1999) 76: 217. doi:10.1023/A:1002001919720

Abstract

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.

amino acid catabolismlactic acid bacteriapeptidasesphysiology

Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • Jeffrey E. Christensen
    • 2
  • Edward G. Dudley
    • 2
  • Jeffrey A. Pederson
    • 1
  • James L. Steele
    • 1
  1. 1.Department of Food ScienceUniversity of Wisconsin-MadisonMadisonUSA
  2. 2.Department of BacteriologyUniversity of Wisconsin-MadisonMadisonUSA