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Mass‐transfer effects on the rate of isomerization of D ‐glucose into D ‐fructose, catalyzed by whole‐cell immobilized glucose isomerase
Author(s) -
Boersma J. G.,
Vellenga K.,
de Wilt H. G. J.,
Joosten G. E. H.
Publication year - 1979
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260211003
Subject(s) - isomerization , chemistry , catalysis , mass transfer , arthrobacter , fructose , glucose 6 phosphate isomerase , isomerase , substrate (aquarium) , kinetics , reaction rate , electron transfer , photochemistry , chromatography , enzyme , organic chemistry , oceanography , physics , quantum mechanics , geology
Abstract 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 electron 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. This structure was subsequently used to describe the reaction including mass‐transfer effects. It appeared that under normal operating conditions the external mass‐transfer rate does not influence the overall rate of reaction. The effect of internal mass‐transfer resistances on the overall reaction rate can well be accounted for by the socalled porous sphere model. The intrinsic kinetics of the isomerization catalyzed by the present catalyst system can be represented by a modified Michaelis–Menten equation for a reversible one‐substrate reaction.