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Detection and localization of peptide hydrolases in Lactobadllus casei

Lactobacillus casei has been isolated from various cheeses (Mabbitt & Zielinska, 1955; Devoyod, 1970; Nath & Ledford, 1973; Dale, 1974) where it develops abundantly (Sharpe, 1962; Fryer, 1969). It is likely that in such ripening cheeses the intracellular proteolytic enzymes play a role in protein breakdown after the death and lysis of the cells. It is therefore important to know the general properties of these enzymes. While proteinases and peptidases of lactic streptococci have already been investigated, similar studies on the proteolytic enzymes of L. casei have been limited. Brandsaeter & Nelson (1956a) showed the presence of a metal activated peptidase system in these bacteria. The fractionation of the crude cell-free extract of L. casei on DEAE-Sephadex was described by Rymaszewski et al. (1974) and the influence of metabolites and cell components of streptococci on the proteolytic activity of L. casei was studied by Libudzisz (1976). Also, Tourneur (1972) showed the presence of cytoplasmic and surface bound activities. A systematic study of the different peptide hydrolases from L. casei would thus be of interest. This paper describes studies of the proteolytic system of L. casei NCDO 151, its localization and the influence of some factors on enzyme production.