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
Hauptverfasser: GALIOTOU-PANAYOTOU, M, RODIS, P, MACRIS, B. J, STATHAKOS, D
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Sprache:eng
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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.
ISSN:0175-7598
1432-0614
DOI:10.1007/BF00250409