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Appl Environ Microbiol. 1971 April; 21(4): 588-593
Copyright © 1971 American Society for Microbiology. All Rights Reserved.
Northern Regional Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Peoria, Illinois 61604
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 Mg2+ were 0.25 and 0.025 M, 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.
1 Presented, in part, at the American Society for Microbiology meeting, Miami Beach, Fla., May 1969.
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