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Properties were determined of the glucose isomerase fromStreptomyces phaeochromogenes NRRL B-3559. The enzyme exhibited a temperature optimum of 80 C and ap H optimum of about 8. The effect of various buffers on activity of the enzyme and the optimump H were studied. Michaelis constants for glucose and Mg2+ were 0.25 and 0.025m , respectively. Co2+ enhanced enzyme activity. A functional polyacrylamide-entrapped glucose isomerase was prepared. The conditions for entrapment and use of the bound enzyme were examined.

Free and Immobilized Glucose Isomerase from Streptomyces phaeochromogenes