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Intrinsic kinetic constants of an immobilised glucose‐isomerase
Author(s) -
Benaiges M. D.,
Solà C.,
De Mas C.
Publication year - 1986
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280361008
Subject(s) - glucose 6 phosphate isomerase , chemistry , michaelis–menten kinetics , kinetic energy , enzyme , isomerization , fructose , isomerase , mass transfer , kinetics , immobilized enzyme , reaction rate constant , chromatography , thermodynamics , enzyme assay , catalysis , biochemistry , physics , quantum mechanics
The isomerization of glucose into fructose using a commercial immobilised glucose‐isomerase has been studied and an initial transitory state of the enzyme, probably due to an establishment of stationary concentration profiles, was observed. Operational conditions to minimise the effects of external and internal mass transfer were determined using immobilised enzyme particles with diameters less than 0.064 mm. Thermal enzyme deactivation of the enzyme was insignificant if it was pre‐treated with cobalt. The intrinsic kinetic constants of the reversible reaction Michaelis—Menten equation were calculated, in operational conditions free of mass transfer effects.