Mass-transfer effects on the rate of isomerization of D-glucose into D-fructose, catalyzed by whole-cell immobilized glucose isomerase.

The investigated catalyst system consists of immobilized Arthrobacter cells containing the enzyme glucose isomerase, which catalyzes the isomerization of glucose into fructose. The internal structure of the catalyst was determined from electrom microscope photographs of replicas of freeze-etched catalyst. On the basis of the photographs a model for the internal structure of the catalyst was proposed.

Combined external and internal mass transfer effects in heterogeneous (enzyme) catalysis.

A graphical method is outlined in order to calculate the conversion under combined intra- and extraparticle transport limitations using the existing effectiveness factor charts for intraparticle diffusion. This method is applied to the case of an immobilized enzyme, assuming that the kinetics are of the Michaelis-Menten type.