Spore lytic enzyme released from Clostridium perfringens spores during germination.
The exudate of fully germinated spores of Clostridium perfringens was found to contain a large amount of a spore lytic enzyme which acted directly on alkali-treated spores of the organism to cause germination. Although no detectable amount of the enzyme was found in dormant spores during germination in a KCl medium, the enzyme was produced rapidly and released into the medium. The optimal conditions for enzyme activity were pH 6.0 and 45 degrees C. Maximum activity occurred in the presence of various univalent cations at a concentration of 50 mM. The enzyme was readily inactivated by several sulfhydryl reagents. A strong reducing condition was generated in the ionic germination of the spores, a minimum Eh level of -350 mV being reached 30 min after initiation of germination. Furthermore, adenosine triphosphate-dependent pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) was identified in both dorman and germinated spores. The relationship between the release of active enzyme and the generation of reducing conditions during germination is discussed.
D002412:Cations; D003016:Clostridium perfringens / Q000201:enzymology* / Q000502:physiology; D010084:Oxidation-Reduction; D013171:Spores, Bacterial / Q000201:enzymology / Q000502:physiology; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013696:Temperature
D002412:Cations; D013439:Sulfhydryl Reagents