Characterization of the autolytic enzymes of Clostridium perfringens

Journal of General Microbiology
R Williamson, J B Ward

Abstract

Clostridium perfringens and isolated walls of this organism autolysed rapidly when incubated in buffer at pH 7.0 with the release of free-reducing groups but no N-terminal amino acids. The predominant autolytic enzyme was an endo-beta-N-acetylglucosaminidase, and an endo-beta-N-acetylmuramidase was also present. The autolytic enzymes could be solubilized by extraction of the organisms with 5 M-LiCl and would then subsequently bind to and rapidly lyse walls of Micrococcus luteus and, more slowly, formamide-extracted walls of C. perfringens and walls of Bacillus subtilis. Lysis of C. perfringens walls by these extracted enzymes could not be demonstrated.

Citations

May 1, 1992·Journal of General Microbiology·C CrouxP Soucaille
Nov 1, 1987·Annales De L'Institut Pasteur. Microbiology·S S Tang, R G Labbe
Jan 16, 1989·Biochemical and Biophysical Research Communications·P GarcíaR López
Apr 1, 1994·Molecular & General Genetics : MGG·B CanardS T Cole

Related Concepts

Beta-N-Acetylglucosaminidase
Cell Wall
Clostridium perfringens
Exoglycosidases
Hydrogen-Ion Concentration
Hydrolysis
Leftose
Polysaccharides

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