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Biol Bull 126: 220-234. (April 1964)
© 1964 Marine Biological Laboratory
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THE PROPERTIES AND SPECIFICITY OF A beta-GLUCOSIDASE FROM BLABERUS CRANIIFER

FRANK M. FISHER JR. 1

1 Department of Biology, Rice University, Houston, Texas

1. The localization, properties and specificity of a beta-glucosidase from Blaberus craniifer have been investigated.

2. The enzyme is localized mainly in the cecal complex of the alimentary canal.

3. Evidence is presented which suggests that all the beta-glucosides hydrolyzed are hydrolyzed by the same enzyme and that the beta-galactosides are hydrolyzed by another protein or series of active sites.

4. The data also suggest that some specificity of the enzyme is directed toward the aglycone moiety of the beta-glucoside.

5. Based on inhibition of the enzyme by heavy metals and specific -SH inhibitors and the reversal of -SH inhibition by cysteine, it is suggested the enzyme is an -SH enzme.

6. No effects of toluene were noted and the effects of monovalent cations were less than 10%.

7. The Km, Vmax and Ki values for various glucosides are presented.







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