Abstract
Selective inhibition of the hydrolysis of p-nitrophenyl-β-D-glucopyranoside (PNPG) catalyzed by β-glucosidase, immobilized in a gelatin membrane, was carried out by use of the complex formation between PNPG and α- or β-cyclodextrin (CD). α- or β-CD showed some suppression only in the hydrolysls of PNPG, and little supPression in the hydrolysis of the o-isomer. Kinetics for the hydrolysis of PNPG in the pfesence of α- or β-CD was identical with that in its absence.
