Enzymatic dynamics of catechol oxidase from Gastrolina depressa |
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Authors: | Yan Zhao Chao-Bin Xue Cheng-Gang Zhou Wan-Chun Luo |
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Institution: | a College of Plant Protection, Shandong Agricultural University, Shandong, Tai’an 271018, PR China b Jinan Forest Bureau of Shandong Province, Shandong, Jinan 250000, PR China c Engineering Research Center of Prevention and Control for Forest Harmful Lives of Shandong Province, Shandong, Tai’an 271018, PR China |
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Abstract: | Properties of the phenoloxidase (PO) from adult of Gastrolina depressa Baly (Coleoptera: Chrysomelidae) as well as effects of some metal ions and inhibitors on the activity of PO purified by (NH4)2SO4 were determined. The optimal pH and temperature of the enzyme for the oxidation of catechol were determined to be at pH 7.5 and at 40 °C, respectively. The kinetic parameters for the oxidation of L-DOPA and catechol by the PO were 15.01 and 9.17 mM, respectively. The PO activity was strongly inhibited by Zn2+ and Cu2+, different to Mg2+ slightly. Both ascorbic acid and cysteine exhibited competitive inhibition and the inhibitory constants (Ki) were determined to be 2.22 mM and 0.40 mM, respectively. |
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Keywords: | Inhibitory mechanism Gastrolina depressa Phenoloxidase (PO) Ascorbic acid Cysteine Property |
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