Isolation and characterization of a nitrile hydratase from a Rhodococcus sp
Autor: | Claus Emborg, Carsten M. Hjort, Sven Erik Godtfredsen |
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Rok vydání: | 2007 |
Předmět: |
chemistry.chemical_classification
biology Molecular mass Renewable Energy Sustainability and the Environment Stereochemistry General Chemical Engineering Organic Chemistry Ion chromatography biology.organism_classification Pollution Nitrilase Enzyme assay Inorganic Chemistry chemistry.chemical_compound Fuel Technology Enzyme chemistry Nitrile hydratase Acrylamide biology.protein Organic chemistry Waste Management and Disposal Rhodococcus Biotechnology |
Zdroj: | Journal of Chemical Technology & Biotechnology. 48:217-226 |
ISSN: | 1097-4660 0268-2575 |
DOI: | 10.1002/jctb.280480211 |
Popis: | A new nitrile hydratase producing strain of Rhodococcus has been found. A method for purification of the nitrile hydratase and a characterization of the enzyme is described. The hydratase is a 52-kdal protein consisting of two subunits of molecular weights, 26 and 23 kdal, respectively. The hydratase exhibits a broad substrate specificity. Aliphatic saturated or unsaturated nitriles, as well as aromatic nitriles, are substrates for the enzyme. Inhibition of the enzyme activity by amides and carboxylic acids was observed. The optimum pH of the hydratase is 7.5. The enzyme is rather unstable, even at room temperature. The enzyme may be applied for the production of acrylamide. For this application of the enzyme, the optimal temperature is about 4°C, where the enzyme exhibits a satisfactory activity and stability. |
Databáze: | OpenAIRE |
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