PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR LIPASE ENZYME FROM Aspergillus costaricaensis CBS115574

In the present study, the lipase of alkaline nature obtained from the previously isolated strain Aspergillus costaricaensis CBS115574 was characterized and purified out using ammonium sulfate precipitation and chromatographic techniques on Diethylaminoethyl A-50 and Sephadex G-100. The purified lipase has the molecular weight of ~50 kDa which was determined by Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Zymography by using the phenol red along with the purification fold of 6.63 and specific activity of 31.73 IU/mg after the gel filtration chromatography. Lipase was found to be stabilized at the pH 7 (122.68 IU/g/min) and at the temperature of 80ºC (141.36 IU/g/min) with its optimal activity at pH 8 and temperature 50ºC. The Km and Vmax value for extracellular lipase were reported to be 29.62 mM and 74.07 IU/ml with their higher tolerance to glycerol (organic solvent), tween 80 (detergent), Ethylene diamine tetra acetic acid (activator & inhibitor), hydrogen peroxide (oxidizing & reducing agent) and sodium chloride (metal ions) with lipase activity of 106.74 IU/g/min, 84.53 IU/g/min, 108.06 IU/g/min, 97.17 IU/g/min and 118.7 IU/g/min. The above results suggested that A. costaricaensis CBS115574 lipase found a suitable position for application in different types of industries.