Free and immobilized glucose isomerase from Streptomyces phaeochromogenes.
- 1 April 1971
- journal article
- Vol. 21 (4), 588-93
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.This publication has 9 references indexed in Scilit:
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