[Glucose-isomerizing enzyme from Actinomyces olivocinereus and its immobilization on aminosilochrome].
Glucose-isomerizing enzyme was isolated from the culture of Actinomyces olivocinereus. It was purified by the chromatography on DEAE-cellulose. The samples of glucose-isomerasing enzyme are homogeneous according to the results of analytical electrophoresis and ultracentrifugation. Glucose-isomerase is more stable than soluble one. The pH-optima of soluble and immobilized enzymes are 8.5 and 7.5, respectively. The temperature optimum of immobilized enzyme, Km, V, and activation energy do not change during immobilization. The immobilized sample has 58% activity of soluble enzyme.
D002238:Carbohydrate Epimerases / Q000302:isolation & purification* / Q000378:metabolism; D003035:Cobalt / Q000494:pharmacology; D004355:Drug Stability; D004800:Enzymes, Immobilized; D005947:Glucose; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D012822:Silicon Dioxide; D013302:Streptomyces / Q000201:enzymology*
D004800:Enzymes, Immobilized; D003035:Cobalt; D012822:Silicon Dioxide; D002238:Carbohydrate Epimerases; D008274:Magnesium; D005947:Glucose
Gliukozonzomeraza iz Actinomyces olivocinereus 154 i ee immobilizatsiia na aminirovannom silokhrome.