Hydroperoxide inactivation of enzymes within spores ofBacillus megateriumATCC19213

Autor:	Robert E. Marquis, Glen C. Rutherford, Alfredo Palop
Rok vydání:	1996
Předmět:	chemistry.chemical_classification fungi Aldolase A Enolase Fructose-bisphosphate aldolase Dehydrogenase Biology Protoplast biology.organism_classification Microbiology Spore Enzyme Biochemistry chemistry Genetics biology.protein Molecular Biology Bacillus megaterium
Zdroj:	FEMS Microbiology Letters. 142:283-287
ISSN:	1574-6968 0378-1097
DOI:	10.1111/j.1574-6968.1996.tb08444.x
Popis:	Hydroperoxide inactivation of the protoplast enzymes enolase, aldolase and glucose-6-phosphate dehydrogenase in intact spores of Bacillus megaterium ATCC19213 was assessed by first treating the cells with lethal levels of H2O2, then germinating them in the presence of chloramphenicol prior to permeabilization and enzyme assays. Glucose-6-phosphate dehydrogenase proved to be more sensitive to H2O2than enolase or aldolase, in agreement with findings for isolated enzymes. Average D values (time for 90% inactivation) for spores treated with 0.50% H2O2 were 173 min for enolase, 67 min for aldolase and 32 min for glucose-6-phosphate dehydrogenase, compared with a D value of 34 min for spore killing. H2O2 killing of spores was found to be conditional in that recoveries of survivors were greater on complex medium than on minimal medium. Overall, it appeared that oxidative inactivation of enzymes may be important for hydroperoxide killing of spores.
Databáze:	OpenAIRE
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