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Adsorption of Trichoderma reesei cellulase on cellulose: Experimental data and their analysis by different equations

1988; Wiley; Volume: 32; Issue: 7 Linguagem: Inglês

10.1002/bit.260320703

1097-0290

Walter Steiner, Wolfgang Sattler, H. Esterbauer,

Enzyme Catalysis and Immobilization

Abstract The adsorption of cellulase from Trichoderma reesei MCG 77 on Avicel was measured at varying cellulase (2–8 g/L) and Avicel (10–200 g/L) concentrations at pH 4.8 and 50°C. Different mathematical equations were derived for the evaluation of the experimental data. The fraction of cellulase protein that can maximally be adsorbed is 0.96, and 1 g Avicel can bind maximally 0.092 g cellulase protein. The Michaelis constant for the adsorption equilibrium [cellulase] + [Avicel] ⇌ [cellulase Avicel] complex is between 2.0 and 2.3 · 10 −5 mol/L. This value is based on the assumption that cellulase has an average molecular weight of 48.000. The apparent molecular weight of Avicel, i.e., that amount in grams that can bind 1 mol cellulase, is 520,000. Under maximum binding the enzyme covers on Avicel a surface of 42 m 2 /g, and the occupied volume is 0.186 cm 3 /g Avicel.