Immobilization of D-xylose (D-glucose) isomerase from a Chainia species

• Published in: Preparative biochemistry Vol. 24; no. 2; p. 143
• Main Authors: Pawar, H S, Deshmukh, D R
• Format: Journal Article
• Language: English
• Published: United States 01-05-1994
• Subjects: Actinomycetales - enzymology; Adsorption; Aldose-Ketose Isomerases; Carbohydrate Epimerases - antagonists & inhibitors; Carbohydrate Epimerases - metabolism; Catalysis; Cations, Divalent; Cobalt - pharmacology; Enzyme Stability; Enzymes, Immobilized; Hot Temperature; Hydrogen-Ion Concentration; Magnesium - pharmacology; Resins, Plant; Sorbitol - pharmacology; Substrate Specificity; Temperature; Xylitol - pharmacology
• ISSN: 0032-7484
• DOI: 10.1080/10826069408010088

D-Xylose isomerase is a heat-stable enzyme which isomerizes D-xylose into D-xylulose. D-Xylose isomerase from various species also isomerizes D-glucose into D-fructose. This enzyme is used in industry for the production of high-fructose corn syrup. The enzyme is specific for both, xylose and glucose. In most species xylose isomerase is localized intracellularly. However, in a rare actinomycete, Chainia sp. (NCL 82-5-1), xylose isomerase is present in both intracellular and extracellular compartments. We have previously purified and characterized intracellular enzyme from Chainia sp. In the present paper, we describe a procedure for immobilization of intracellular xylose isomerase on INDION 48-R by ionic binding. This method is inexpensive, does not require cross-linking agents and results in firm binding of the enzyme with the resin. The properties of immobilized enzyme such as pH optimum, substrate specificity, Km and inhibition by various metabolites are described and compared with those of purified, nonimmobilized enzyme.