Purification and Biochemical Properties of Carboxylesterase from Saga Seeds (Adenanthera pavonina)
Автор: Shafia Hoor F., Nagesh Babu R.
Журнал: Журнал стресс-физиологии и биохимии @jspb
Статья в выпуске: 1 т.17, 2021 года.
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Carboxyl esterase (E.C.No.3.1.1.1) was partially purified from Adenanthera pavonina (Saga) using ammonium sulfate fractionation (0-60%) and DEAE (diethyl aminoethyl) ion exchange chromatography, the purified enzyme was characterized. One major saga-esterase was identified with Fold purification of 29. Molecular weight of the Ap-esterase was determined using Sephadex G-25 gel filtration and SDS-PAGE (Sodium dodecyl sulfate polyacryamide gel electrophoresis) which was found to be 26.0 k Da. Optimal activity of the saga-esterase occurred when the pH 7.0 at a temperature of 55°C. The activation energy for the hydrolysis of α-naphthyl acetate was determined to be 1.10 kcal/ mol. The Michaelis Menton constant (Km) and Vmax of the saga-esterase was 0.4µmoles and 105 IU respectively. In addition, the isoelectric point is at pH > 9 and immuno-blot using polyclonal antibodies showed that the saga-esterase was widely distributed in seeds but not in leaves. The saga-esterase inhibited by organophosphate and carbamate pesticides, which can be substituted for acetylcholinesterase.
Carboxyl esterase, Adenanthera pavonina, Organophosphate, carbamate pesticide
Короткий адрес: https://sciup.org/143173876
IDR: 143173876
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