Modulation of the cell-surface proteinase activity of thermophilic lactobacilli by the Peptide supply.

HÉBERT EM, RAYA RR, DE GIORI GS.

CURRENT MICROBIOLOGY

SPRINGER

Lugar: New York, NY 10013; Año: 2002 vol. 45 p. 385 - 389

0343-8651

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 alpha- and beta-casein degradation, four types of P(III)-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.