Open AccessHydroperoxide inactivation of enzymes within spores of Bacillus megaterium ATCC19213
Author(s) -
Palop Alfredo,
Rutherford Glen C.,
Marquis Robert E.
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08444.x
Subject(s) - aldolase a , bacillus megaterium , spore , enolase , biochemistry , enzyme , dehydrogenase , fructose bisphosphate aldolase , biology , lactate dehydrogenase , microbiology and biotechnology , chemistry , bacteria , genetics , immunohistochemistry , immunology
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 H 2 O 2 , then germinating them in the presence of chloramphenicol prior to permeabilization and enzyme assays. Glucose‐6‐phosphate dehydrogenase proved to be more sensitive to H 2 O 2 than enolase or aldolase, in agreement with findings for isolated enzymes. Average D values (time for 90% inactivation) for spores treated with 0.50% H 2 O 2 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. H 2 O 2 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.