THE CLEAVAGE OF ADENOSINE BY SPORES OF BACILLUS CEREUS

Abstract

Clean dry spores of B. cereus var. terminalis catalyze the cleavage of adenosine into adenine and ribose, apparently without involvement of phosphate. The amount of sugar recovered is insufficient to account for all of the adenosine cleaved. The optimum pH of the reaction is near pH 5. The reaction has an energy of activation of 11,500 cal., with an optimum temperature near 90[degree]C and a Michaelis-Menten constant of 1.0 xlO-3 [image]. The apores retain 50% activity after 4 hours at 100[degree]C, but the activity is lost after autoclaving the spores at 121[degree] C for 15 minutes.