Flow kinetics of immobilized β-glucosidase

Glucoamylase has been covalently immobilized in controlled pore glass fibers packed parallel to the axis of a tubular reactor. Flow kinetic studies have been carried out for a range of flow rates and substrate concentrations at 50 "C and pH 4.5. Diffusion control has been found negligible with high flow rates and substrate concentrations. The apparent MICHAELIS constant was three orders of magnitude higher than that of the free enzyme. As flow rate and substrate concentration decrease, the extent of diffusion control increased up to a moderate degree. The immobilized glucoamylase was more stable than the free enzyme when incubated at 50 "C.

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“…mus attached to tubes. These methods have been tested with L-asparaginase [I 21 and /Lglucosidase [13] attached to nylon tubing.…”

Section: Introductionmentioning

confidence: 99%

Maltose hydrolysis kinetics with glucoamylase immobilized in porous glass fibers in a tubular flow reactor

Toldrá

Jansen

Tsao

1990

Nahrung

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Hydrolysis of cellobiose using β‐glucosidase from Penicillium funiculosum. Kinetic analysis

Romero

Aguado

Rodríguez

et al. 1999

Acta Biotechnologica

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The kinetics of cellobiose hydrolysis was studied using Pglucosidase from Prnicilliumfuniculosum, both free and immobilized on nylon powder, at different temperatures, pH values, enzymatic activities and initial cellobiose and glucose concentrations. The experimental results were fitted to a kinetic model by considering the substrate and product inhibitions as well as the thermal deactivation of Pglucosidase with a mean deviation of less than 10%. The immobilization of Pglucosidase led to an increase in the stability of the enzyme against changes in the pH value.

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