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Glucose isomerase immobolized on porous glass
Author(s) -
Lee Y. Y.,
Fratzke A. R.,
Wun K.,
Tsao G. T.
Publication year - 1976
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.260180309
Subject(s) - glucose 6 phosphate isomerase , catalysis , chemistry , fructose , porous glass , porosity , reaction rate , enzyme , immobilized enzyme , isomerase , reaction rate constant , enzyme catalysis , chromatography , kinetics , thermodynamics , organic chemistry , physics , quantum mechanics
Partially purified glucose isomerase from a Streptomyces species was immobilized on porous glass particles and studied for various characteristics concerning its use as an industrial catalyst. The activities were investigated in relation to the reaction parameters and the enzyme deactivation was studied systematically under various reaction conditions. The half‐life of the immobilized enzyme was found to exceed 200 days at 50°C. The rate equation of the reversible glucose ⇄ fructose reaction was derived and the kinetic constants were determined. The rate equation was found to be in good agreement with experimental data for both forward and reverse reactions. The degree of diffusional effects was experimentally measured and theoretically analyzed.