Free and Immobilized Glucose Isomerase from <i>Streptomyces phaeochromogenes</i>

Abstract

Properties were determined of the glucose isomerase from Streptomyces phaeochromogenes NRRL B-3559. The enzyme exhibited a temperature optimum of 80 C and a pH optimum of about 8. The effect of various buffers on activity of the enzyme and the optimum pH were studied. Michaelis constants for glucose and Mg(2+) were 0.25 and 0.025 m, respectively. Co(2+) enhanced enzyme activity. A functional polyacrylamide-entrapped glucose isomerase was prepared. The conditions for entrapment and use of the bound enzyme were examined.