Purification of a novel enzyme involved in catechin degradation by Calvatia gigantea
Autor: | D. Stathakos, M. Galiotou-Panayotou, B. J. Macris, P. Rodis |
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Rok vydání: | 1988 |
Předmět: |
chemistry.chemical_classification
Chromatography Molecular mass Catechin General Medicine Biology Calvatia gigantea Applied Microbiology and Biotechnology Electrophoresis chemistry.chemical_compound medicine.drug_formulation_ingredient Enzyme Biochemistry chemistry Polyphenol medicine Tannin Specific activity Biotechnology |
Zdroj: | Applied Microbiology and Biotechnology. 28 |
ISSN: | 1432-0614 0175-7598 |
DOI: | 10.1007/bf00250409 |
Popis: | A novel enzyme, involved in the degradation of catechin by Calvatia gigantea, was purified 114-fold over the crude extract yielding 24% purified enzyme with a specific activity 16.1 U/mg protein. Two isozymic forms (I and II) were isolated, both exhibiting the same kinetic characteristics with maximum activity at pH 8 and 35°C. SDS electrophoresis of I and II revealed the presence of two identical components in each form with molecular weights 50 500 and 49 500. |
Databáze: | OpenAIRE |
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