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Clostridium perfringens--specific lysin
Canadian Journal of Microbiology
|May 1, 1977
Abstract:
A mitomycin C induced lysate of Clostridium perfringens strain KZ219 was lytic to 50 strains of C. perfringens of types A-E, and three strains of C. plagarum. The lysin was active against only 2 out of 87 strains of 51 other clostridial species. The optimum pH of the lytic agent was 5.5. The activity was largely inactivated by proteolytic enzymes, and nearly completely inactivated by heating at 60 degrees C for 5 min.
Insights
A Clostridium perfringens lysate showed lytic activity against many C. perfringens strains and some C. plagarum strains. This specific lysin demonstrated limited activity against other clostridial species.
Area of Science:
- Microbiology
- Bacteriology
- Enzymology
Background:
- Clostridium perfringens is an important bacterial pathogen.
- Bacteriophages and their derived lysins are explored for antimicrobial applications.
Purpose of the Study:
- To characterize a lytic agent derived from Clostridium perfringens strain KZ219.
- To determine the spectrum of activity and optimal conditions for this lysin.
Main Methods:
- Induction of a bacterial lysate from C. perfringens using mitomycin C.
- Testing the lytic activity of the lysate against various C. perfringens strains and other clostridial species.
- Assessing the effect of pH, proteolytic enzymes, and heat on lysin activity.
Main Results:
- The lysate was lytic to 50 strains of C. perfringens (types A-E) and 3 strains of C. plagarum.
- The lysin showed limited activity against only 2 out of 87 strains from 51 other clostridial species.
- Optimal lytic activity occurred at pH 5.5.
- Activity was significantly reduced by proteolytic enzymes and heat (60°C for 5 min).
Conclusions:
- The induced lysate contains a specific lysin with potent activity against C. perfringens.
- This lysin exhibits a narrow spectrum of activity, primarily targeting C. perfringens and closely related species.
- The lytic agent's sensitivity to enzymes and heat suggests a protein-based nature.