ISOLATION AND CHARACTERIZATION OF FATTY ACID DESATURASE FROM LOCAL STRAIN OF MICROALGAE CHLORELLA VULGARIS

In this study, desaturase from novel strain of micro algae was isolated and purified. Three step purification procedure i.e., ammonium sulphate precipitation, dialysis and gel filtration chromatography yielded 11 % activity with a purification factor of 2.39. The final enzyme preparation was homogeneous as judged by SDS-polyacrylamide gel electrophoresis having a single polypeptide of 15kDa with 18.033% oil contents. The catalysis of stearoyl-CoA by desaturase was expressed by the Michaelis-Menten equation, exhibiting maximum activity at 37˚C, 7.0 pH and retained its activity for 24h within 5-8 pH range. It was observed that maximum velocity (Vmax) was 13.91 U/mL and Michaelis constant was 0.6 µM revealing a binding site with higher substrate affinity. Furthermore, the present findings will reveal new vistas in the exploitation of Chlorella vulgaris for marvellous desaturase because to our knowledge it is first report for the isolation and characterization of desaturase from micro-algae Chlorella vulgaris.