| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2010120 | Pesticide Biochemistry and Physiology | 2010 | 6 Pages |
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.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Agronomy and Crop Science
Authors
Yan Zhao, Chao-Bin Xue, Long Yang, Cheng-Gang Zhou, Wan-Chun Luo,