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Peptide hydrolases of Lactobacillus casei: isolation and general properties of various peptidase activities

Published online by Cambridge University Press:  01 June 2009

Morsi El Soda ,
Michel J. Desmazeaud  and
J.-L. Bergère
Morsi El Soda
Affiliation:
Laboratoire de Biochimie Microbienne, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France
Michel J. Desmazeaud
Affiliation:
Laboratoire de Biochimie Microbienne, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France
J.-L. Bergère
Affiliation:
Laboratoire de Biochimie Microbienne, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France
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Summary

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 °C for the aminopeptidase, at 30 °C for the dipeptidase and at 40 °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.

Type
Original Articles
Information
Journal of Dairy Research , Volume 45 , Issue 3 , October 1978 , pp. 445 - 455
Copyright
Copyright © Proprietors of Journal of Dairy Research 1978

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References

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