D-Xylose isomerase is a heat-stable enzyme which isomerizes D-xylose i
nto D-xylulose. D-Xylose isomerase from various species also isomerize
s D-glucose into D-fructose. This enzyme is used in industry for the p
roduction of high-fructose corn syrup. The enzyme is specific for both
, xylose and glucose. In most species xylose isomerase is localized in
tracellularly. However, in a rare actinomycete, Chainia sp. (NCL 82-5-
1), xylose isomerase is present in both intracellular and extracellula
r compartments. We have previously purified and characterized intracel
lular enzyme from Chainia sp. In the present paper, we describe a proc
edure for immobilization of intracellular xylose isomerase on INDION 4
8-R by ionic binding. This method is inexpensive, does not require cro
ss-linking agents and results in firm binding of the enzyme with the r
esin. The properties of immobilized enzyme such as pH optimum, substra
te specificity, Km and inhibition by various metabolites are described
and compared with those of purified, nonimmobilized enzyme.