[beta-Glucosidases specific for the cyanogenic glucoside triglochinin from Alocasia macrorrhiza Schott: further characterization of properties (author's transl)].

All beta-glucosidases extracted and separated from a plant of Alocasia macrorrhiza are almost entirely specific for triglochinin. The hexameric beta-glucosidase has been shown to dissociate in dimers without any alteration of activity. Reaggregation could only be demonstrated using bifunctional reagents like glutaraldehyde. Treatments of beta-glucosidase with various chemicals (e. g. glutaraldehyde, dodecyl sulfate) decreased the activity for triglochinin more than the activity for 4-nitrophenyl glucoside. On the other hand, specific reagents like bromocondurite or p-chloromercuribenzoate caused identical inactivations measured with various substrates. It seems possible that the different beta-glucosidases splitting triglochinin arose during purification from the hexameric form which occurs in the plant.