Purification of a novel enzyme involved in catechin degradation by Calvatia gigantea
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 maxi...
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Veröffentlicht in: | Applied microbiology and biotechnology 1988-07, Vol.28 (6), p.543-545 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | 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 degree 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. |
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ISSN: | 0175-7598 1432-0614 |
DOI: | 10.1007/BF00250409 |