THE PROPERTIES AND SPECIFICITY OF A β-GLUCOSIDASE FROM BLABERUS CRANIIFER

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Abstract
Enzymatic activity is largely localized in the cecal complex. By ethanol-acetone precipitation the specific activity was increased some 37-fold. The pH optimum was found to be 5.0 and the energy of activation was 9400 cal/mole. Cellobiose, phenyl-[beta]-D-glucoside, [image]-nitro-phenyl-[beta]-D-glucoside, salicin, and arbutin were hydrolyzed and this hydrolytic activity was decreased proportionally when the enzyme was partially inactivated by heat. Enzymatic activity was inhibited by various - SH inhibitors and this inhibition was partially reversed by the addition of cysteine. No effect of toluene was noted and there was a small stimulatory effect of monovalent cations. Salts of Ag+, Hg+. Hg++, Cu++, Pb++ and Fe++ inhibited hydrolysis in excess of 40%. The Km, Vm and K1 values for various glucosides are presented.