In this piece of work we present the results obtained from the kinetic
study of the fructose-glucose isomerization using the enzyme D-xylose
-ketol-isomerase in soluble form at pH 7.5. The temperature has been v
aried within the 40 to 60-degree-C range, as has the total hexose conc
entration between 0.5 and 2.0 M. The analysis carried out on the influ
ence of the enzyme concentration shows that the conversion reached dep
ends on the C(E).t intensive factor (enzyme concentration . reaction t
ime). The fructose-glucose enzymatic isomerization is a reversible rea
ction which goes through the following mechanism: [GRAPHICS] This mech
anism leads to the following kinetic expression in terms of the conver
sion, x [GRAPHICS] On applying this expression to kinetic experiments,
it has been observed that K(b) almost-equal-to 0, which would imply t
hat the isomerization reaction is in fitting with pseudo first-order k
inetics, meaning that the Michaelis-Menten constants are practically t
he same in both directions and, thus, that the affinity of both isomer
s by the enzyme is very close. We have determined the elementary kinet
ic constants of the isomerization reaction, the following equations be
ing obtained in terms of temperature [GRAPHICS]