A. Converti et M. Delborghi, KINETICS OF GLUCOSE ISOMERIZATION TO FRUCTOSE BY IMMOBILIZED GLUCOSE-ISOMERASE IN THE PRESENCE OF SUBSTRATE PROTECTION, Bioprocess engineering, 18(1), 1998, pp. 27-33
The activity of immobilized glucose isomerase of Streptomyces murinus
has been tested batchwise under different conditions in order to gathe
r the related kinetic parameters necessary to optimize an immobilized
enzyme column for the continuous production of high fructose corn syru
p (HFCS). To this purpose, the Briggs-Haldane model incorporating an a
pparent first-order inactivation constant has been used with success.
A comparison of the equilibrium constants and of the maximum theoretic
al conversion yields calculated at different temperatures with those e
stimated for the native enzyme demonstrates that the immobilization fa
vours the transformation of glucose to fructose only at T > 70 degrees
C, as a possible consequence of a combined effect of catalysis and eq
uilibrium thermodynamics enhancement. Enzyme inactivation has also bee
n tested at different temperatures and sugar concentrations to evaluat
e the related kinetic parameters under different conditions of substra
te protection.