TY  - JOUR
AU  - Shafia Hoor, F.
AU  - Nagesh Babu, R.
T1  - Purification and Biochemical Properties of Carboxylesterase from Saga Seeds (Adenanthera pavonina)
JO  - Journal of Stress Physiology & Biochemistry
Y1  - 2021/march
VL  - 17
IS  - 1
SP  - 47
EP  - 53
UR  - http://www.jspb.ru/issues/2021/N1/JSPB_2021_1_47-53.pdf
KW  - Carboxyl esterase
KW  - Adenanthera pavonina
KW  - Organophosphate
KW  - carbamate pesticide
U1  - 1997-0838
N2  - 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.
ER  -