NDLI: Modulation of the Cell-Surface Proteinase Activity of Thermophilic Lactobacilli by the Peptide Supply

Content Provider	Springer Nature Link
Author	Hébert, Elvira M. Raya, Raul R. de Giori, Graciela Savoy
Copyright Year	2002
Abstract	The proteolytic system of thermophilic lactobacilli is considered important for bacterial nutrition as well as for the formation of flavor and texture in fermented products. We investigated the influence of peptide content on the cell surface proteinase and intracellular aminopeptidase activities from seven thermophilic lactobacilli strains. The proteinase activities were remarkably reduced in cells grown in the peptide-rich medium MRS or in a chemically defined medium supplemented with Casitone compared with those found in a synthetic medium. The degree of inhibition observed was strain dependent. When proteinase activities were analyzed by their hydrolytic patterns of α- and β-casein degradation, four types of PIII-caseinolytic cleavage specificity were distinguished. Lactobacillus helveticus strains possessed aminopeptidase activities with broader specificity than those found in L. delbrueckii subsp. lactis strains. However, the aminopeptidase activities were not influenced by the peptide content of the medium.
Starting Page	385
Ending Page	389
Page Count	5
File Format	PDF
ISSN	03438651
Journal	Current Microbiology
Volume Number	45
Issue Number	6
e-ISSN	14320991
Language	English
Publisher	Springer-Verlag
Publisher Date	2002-12-01
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Medicine Microbiology Applied Microbiology and Biotechnology

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