Purification of a novel enzyme involved in catechin degradation by Calvatia gigantea |
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| Authors: | M Galiotou-Panayotou P Rodis B J Macris D Stathakos |
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| Institution: | (1) Biology Institute, N.R.C. Democritos, Aghia Paraskevi, 15310 Attiki, Greece;(2) Present address: Department of Science and Technology of Food and Agricultural Products, Agricultural University of Athens, Votanikos, Athens, Greece |
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| Abstract: | Summary 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. |
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