| Literature DB >> 5575565 |
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.Entities:
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Year: 1971 PMID: 5575565 PMCID: PMC377236 DOI: 10.1128/am.21.4.588-593.1971
Source DB: PubMed Journal: Appl Microbiol ISSN: 0003-6919