Isolation and Characterization of Clostridium Perfringens Spore-Lytic Enzymes.

摘要

For many years there has been an active interest in the research community on the mechanism by which bacterial spores germinate. The structure of the spore backbone requires that a lytic enzyme be activated during germination in order to allow the core protoplast to be released and resume vegetative cell growth. The question we sought to answer is what role to spore-lytic enzymes play in the germination process of this organism. What is the nature of such enzymes, their location, properties, modes of action, method of activation, etc. IP hydrolysed spore cortical fragments with the release of free amino groups. End group analysis of hydrolysed fragments indicated the presence of N-terminal alanine but not reducing sugars. Molecular cortical fragments indicated that IP acts only on peptidoglycan chains containing cross-lined peptide subunits. IP failed to hydrolyse a number of nitrophenyl-conjugated glucopyranosides and galactopyranosides. The results indicate that IP is an N-acetylmuramyl-L-alanine amidase. Peptidoglycan Hydrolase, An intracellular spore-lytic enzyme (SLE) which causes the germination of spores of Clostridium perfringens has been extracted, partially purified, and characterized. Because intracellular SLE was found in vegetable cells as well as sporulating cells and mutant cells blocked at sporulation state of 0 of C. perfringens, this enzyme may not be spore specific. An investigation was made of the effect of this enzyme on vegetative cell walls and determined its mode of action. Keywords: Bacterial spores; Amino groups; Enzymes; Peptidoglycan hydrolase; Clostridium perfringens. (kt)