Kinetic study on the β-glucosidase-catalysed reaction of Trichoderma viride cellulase
A kinetic study of the β-glucosidase-catalysed reaction of a commercial cellulase preparation from Trichoderma viride is described. The Km and Vmax values of the β-glucosidase system were: (a) 0.5 mm and 6.6 μmol/min, respectively, using p-nitrophenyl β-d-glucopyranoside (pNPG) as substrate; and (b) 2.5 mm and 8.1 μmol/min, respectively, using cellobiose as subtrate. The glucose effect on initial reaction velocity agrees with a mixed-inhibition pattern. The inhibition constant (Ki) values were, 0.53 and 0.39 mm with nNPG and cellobiose as substrates, respectively. The temperature and pH optima were determined.
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