The extremely &hemophilic organism Thermus quaticus possesses high activities of enzymes catalysing the degradation of xyians and metabolizing ~x y l o s e via the pntose phosphate pathway. The D-xylsse isomerase (Dxylsse ketoll-isomerase, EC 5 o 3 o I . 51, an important enzyme of this process, is efficiently induced by its substrate Dxylose, and, 40 a lesser extent, by related pentoses and some derivatives of 1p-xylose. The ~-xyPose isomerase from T. qrsatkus has been g u~e d by anion-exchange chrmmtography, chromatography on ID-xylkose agarose and gcE filtration. A single band migrating according to an Mr of 5 0 0 was obtained by SDS-PAGE. An M,. oh 194800 for the native enzyme, determined by gel filtration and ultracentrifugation in a glycerol gradient, suggested that the Dxylsw isomerase is a homomeric tetramer. Amhenius plots of the enzyme activity of the D-xylose isomerase weref linear up to a temperature of $5 OC. At 90 "C the enzyme was inactivated in the absence of divalent c;~PPoRs, with a haIf4ife of 4 d, while in the presence of Mn2+ or Co2+ it remained fully active for at least 1 mo~ith. The enzyme $ilia2 an isoelectric point at 4.4 and showed a broad optimum in the pH range from 5-5 to 8-5. NQ significant difkepemces in the pH and temperature behaviour could be observed when ~x y l o s e was compared with D -~~U C Q W as substrate. Digearen& methods of immobilization of the enzyme to solid supports as well as inclusion into nyhm beads w m studied. Attachment of the enzyme to epoxy-activated agarose and its m-aggregation with bovine serum albumin gave immobilized preparations with the same stability as free enzyme supplemente i t h hh2+ QP cQ*+e