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The isomerization of D ‐glucose into D ‐fructose catalyzed by whole‐cell immobilized glucose isomerase. The dependence of the intrinsic rate of reaction on substrate concentration, pH, and temperature
Author(s) -
Kikkert A.,
Vellenga K.,
de Wilt H. G. J.,
Joosten G. E. H.
Publication year - 1981
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.260230516
Subject(s) - isomerization , fructose , substrate (aquarium) , chemistry , catalysis , isomerase , glucose 6 phosphate isomerase , reaction rate , biochemistry , biophysics , enzyme , biology , ecology
The relation between the intrinsic rate of the glucose‐fructose isomerization catalyzed by whole‐cell immobilized glucose isomerase and the substrate concentration can be described with the kinetic modelThe numerical values of k 1 , k −1 , k 2 , and k −2 have been determined from low‐conversion experiments starting from pure glucose or fructose solutions, and are presented as a function of pH and temperature. The difference between the overall chemical reaction rate determined in high‐conversion experiments and that calculated from the individual k 1 , k −1 , k 2 , and k −2 values is less than 10%.