Peptide hydrolases of Lactobacillus casei: isolation and general properties of various peptidase activities.
J Dairy Res, 1978/10;45(3):445-55.
El Soda M, Desmazeaud MJ, Bergère JL
PMID: 101561
Impact factor: 2.027
Abstract
Discovery of an endopeptidase by gel chromatography and separation of 3 exopeptidases (a dipeptidase, an aminopeptidase and a specific carboxypeptidase) from Lactobacillus casei NCDO 151 by affinity chromatography is described. The 3 exopeptidases were strongly inhibited by the metal chelators EDTA and 1,10-phenanthroline but were reactivated with Co2+ and Mn2+. The pH optima for aminopeptidase, dipeptidase and carboxypeptidase activities were 6.5, 7.6 and 7.2, respectively. Maximum activity was obtained at 45 degrees C for the aminopeptidase, at 30 degrees C for the dipeptidase and at 40 degrees C for the carboxypeptidase. The substrate specificities of the 3 enzymes were also studied. The properties of these 3 enzymes are compared with those of other bacteria.
MeSH terms
Aminopeptidases; Carboxypeptidases; Dipeptidases; Drug Stability; Endopeptidases; Kinetics; Lactobacillus casei; Peptide Hydrolases; Substrate Specificity
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