Rudee SuraritHirokazu MatsuiSeiya ChibaJisnuson SvastiChantragan SrisomsapMahidol UniversityHokkaido UniversityChulabhorn Research Institute2018-07-042018-07-041997-01-01Bioscience, Biotechnology and Biochemistry. Vol.61, No.1 (1997), 93-9513476947091684512-s2.0-0030896424https://repository.li.mahidol.ac.th/handle/123456789/17925Kinetic 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 Kiof 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 Kmand apparent Vmaxat 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. © 1997, Taylor & Francis Group, LLC. All rights reserved.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyChemistryImmunology and MicrobiologyArticleSCOPUS10.1271/bbb.61.93