Purification and Characterization of Cell Suspensions Peroxidase from Cotton (<Emphasis Type="Italic">Gossypium hirsutum</Emphasis> L.) |
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Authors: | Tanoh Hilaire Kouakou Edmond Ahipo Dué N’guessan Eugène Jean Parfait Kouadio Sébastien Niamké Yatty Justin Kouadio Jean-Michel Mérillon |
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Institution: | Tanoh Hilaire Kouakou, Edmond Ahipo Dué, N’guessan Eugène Jean Parfait Kouadio, Sébastien Niamké, Yatty Justin Kouadio and Jean-Michel Mérillon |
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Abstract: | Two peroxidases, cPOD-I and rPOD-II, have been isolated and purified from cotton cell suspension and their biochemical characteristics
studied. rPOD-II from R405-2000, a non-embryogenic cultivar, has higher activity than cPOD-I derived from Coker 312, which
developed an embryogenic structure. The cPOD-I and rPOD-II had molecular mass of 39.1 and 64 kDa respectively, as determined
by SDS-PAGE. Both enzymes showed high efficiency of interaction with the guaiacol at 25 mM. The optimal pH for cPOD-I and
rPOD-II activity was 5.0 and 6.0, respectively. The enzyme had an optimum temperature of 25 °C and was relatively stable at
20–30 °C. The isoenzymes were highly inhibited by ascorbic acid, dithiothreitol, sodium metabisulfite, and β-mercaptoethanol.
Their activities were highly enhanced by Al3+, Fe3+, Ca2+, and Ni2+, but they were moderately inhibited by Mn2+ and K+. The enzyme lost 50% to 62% of its activity in the presence of Zn2+ and Hg2+. |
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Keywords: | Gossypium hirsutum L Cell suspension Peroxidase Purification Characterization |
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