Purification and characterization of an intracellular peroxidase from Streptomyces cyaneus
Article Abstract:
An intracellular peroxidase was isolated from Streptomyces cyaneus, and was purified by anion-exchange chromatography and gel filtration followed by preparative isoelectic focusing. The purified enzyme was a dimer composed of equal subunits having molecular weights of 92 kDa. Further characterization showed that the enzyme had both peroxidase and catalase activities. Spectrographic and enzyme inhibition analysis showed that the enzyme is a hemoprotein. The K(sub m) of the peroxidase for o-diansisidine was 17.8 micromolar, while the catalase had a K(sub m) for hyrogen peroxide at 2.07 millimolar.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
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Enzymatic conversion of glucose to UDP-4-keto-6-deoxyglucose in Streptomyces spp
Article Abstract:
A study was conducted to analyze the enzymatic transformation of glucose to UDP-4-keto-6-deoxyglucose in Streptomyces spp. The pathway of sugar activation in Streptomyces spp. supported glucose 6-phosphorylation by hexokinase. High-performance liquid chromatography was carried out using a Rheodyne injector type 7125 with a 100-micron-l loop linked to a model LC-6A pump. Centrifugations were then performed with a Sorvall RC-5 refrigerated centrifuge.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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Purification and characterization of 2,6-beta-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2
Article Abstract:
An enzyme has been isolated from Streptomyces exfoliatus that not only hydrolyzes the beta-2,6-linkage of levan but also the beta-2,1-linkage of fructooligosaccharides. The properties of the enzyme are discussed.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
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