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

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.