Mar 26, 1990

Kinetic mechanism of beta-glucosidase from Trichoderma reesei QM 9414

Biochimica Et Biophysica Acta
P EstradaC Acebal


beta-Glucosidase is a key enzyme in the hydrolysis of cellulose to D-glucose. beta-Glucosidase was purified from cultures of Trichoderma reesei QM 9414 grown on wheat straw as carbon source. The enzyme hydrolyzed cellobiose and aryl beta-glucosides. The double-reciprocal plots of initial velocity vs. substrate concentration showed substrate inhibition with cellobiose and salicin. However, when p-nitrophenyl beta-D-glucopyranoside was the substrate no inhibition was observed. The corresponding kinetic parameters were: K = 1.09 +/- 0.2 mM and V = 2.09 +/- 0.52 for salicin; K = 1.22 +/- 0.3 mM and V = 1.14 +/- 0.21 for cellobiose; K = 0.19 +/- 0.02 mM and V = 29.67 +/- 3.25 for p-nitrophenyl beta-D-glucopyranoside. Studies of inhibition by products and by alternative product supported an Ordered Uni Bi mechanism for the reaction catalyzed by beta-glucosidase on p-nitrophenyl beta-D-glucopyranoside as substrate. Alternative substrates as salicin and cellobiose, a substrate analog such as maltose and a product analog such as fructose were competitive inhibitors in the p-nitrophenyl beta-D-glucopyranoside hydrolysis.

Mentioned in this Paper

4-nitrophenyl beta-D-glucoside ion (1-)
Trichoderma reesei
4-nitrophenol, sodium salt, (2: 1), dihydrate

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