Purification of a novel enzyme involved in catechin degradtion by Calvatia gigantea
1988
Galiotou-Panayotou, M. | Rodis, P. | Macris, B.J. | Stathakos, D.
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 49500.
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