Abstract
Kinetic analyses have been done on the hydrolysis of p-nitrophenyl β-d-glucoside (PNPG) and p-nitrophenyl β-d-fucoside (PNPF) by the β-d-glucosidase/ β-d-fucosidase enzyme from Thai Rosewood (Dalbergia cochinchinensis Pierre). PNPF showed a competitive inhibition of PNPG hydrolysis with a Ki of 0.42 mm. Hydrolysis of mixtures of PNPG and PNPF at fractional ratios ranging from 0 to 1 showed Lineweaver–Burk plots intermediate between the two extremes. The apparent Km and apparent Vmax at each fractional ratio showed good correspondence with the theoretical curves predicted for the existence of a single common active site for the hydrolysis of the two substrates.
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