Purification and Biochemical Characterization of Polyphenol Oxidases from Embryogenic and Nonembryogenic Cotton (<Emphasis Type="Italic">Gossypium hirsutum</Emphasis> L.) Cells |
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Authors: | Tanoh Hilaire Kouakou Yatty Justin Kouadio Patrice Kouamé Pierre Waffo-Téguo Alain Décendit Jean-Michel Mérillon |
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Institution: | Groupe d'Etude des Substances Végétales à Activités Biologiques, Institut des sciences de vigne et du Vin, UFR des Sciences Pharmaceutiques, Université de Bordeaux 2, 146 rue Léo-Saignat, 33076 Bordeaux cedex, France. |
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Abstract: | Polyphenol oxidases (PPOs) were isolated from cell suspensions of two cultivars of cotton (Gossypium hirsutum L.), and their biochemical characteristics were studied. PPO from Coker 312, an embryogenic cultivar, showed a highest affinity
to catechol 20 mM, and PPO from R405-2000, a nonembryogenic cultivar, showed a highest affinity to 4-methylcatechol 20 mM.
The optimal pH for PPO activity was 7.0 and 6.0 for Coker 312 and R405-2000, respectively. The enzyme had an optimal temperature
of 25 °C and was relatively stable at 20–30 °C. Reducing sodium metabisulfite, ascorbic acid, dithiothreitol, SnCl2, and FeCl3 markedly inhibited PPO activity, whereas its activity was highly enhanced by Mg2+, Ca2+, and Mn2+ and was moderately inhibited by Ba2+, Cu2+, and Zn2+. The analysis revealed a single band on the sodium dodecyl sulfate polyacrylamide gel electrophoresis which corresponded
to a molecular weight of 55 kDa for Coker 312 and 42 kDa for R405-2000. |
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Keywords: | Cell suspension Characterization Cotton Gossypium hirsutum L Polyphenol oxidase Purification |
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