Free and Immobilized Glucose Isomerase from Streptomyces phaeochromogenes1
AUTOR(ES)
Strandberg, Gerald W.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=377236Documentos Relacionados
- D-Glucose Isomerase: Constitutive and Catabolite Repression-Resistant Mutants of Streptomyces phaeochromogenes
- Immobilization of Glucose Isomerase-Containing Streptomyces phaeochromogenes Cells in Fine-Particle Form
- Extraction of glucose isomerase from Streptomyces flavogriseus.
- Studies on glucose isomerase from a Streptomyces species.
- Purification, Immobilization, and Some Properties of Glucose Isomerase from Streptomyces flavogriseus†
