Purification and Characterization of Hydroperoxidelyase from soybean (Glycine max)
نویسنده
چکیده
A fatty acid hydroperoxidelyase (HPL) enzyme from soybean (Glycine max) seeds was purified by ammonium sulphate precipitation followed by ion exchange chromatography on DEAE-Cellulose and DEAE-Sephacel. HPL showed specific activity of 161U/mg with fold purification of 16.4 and enzyme yield was found to be 9.06%. The purified enzyme on SDSPAGE showed a prominent band of ~53KDa. Kinetic studies were carried out for the HPL enzyme which revealed Vmax and Km value of 275.48 x 10-3 ΔOD/min and 25μm respectively. Natural antioxidants of soybean such as α-tocopherol, genistein, glycetein, daidzein and ascorbic acid were subjected under In vitro studies to analyse inhibitory effect on the enzyme. Among all the natural antioxidants, ascorbic was found to be potent inhibitor with IC50 value 39.25 μm.
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