PURIFICATION AND CHARACTERIZATION OF LIPASE FROM THERMOPHILIC BACTERIAL CONSORTIUM

Abstract

The purification and characterization of lipase from a thermophilic bacterial consortium is crucial
for developing robust biocatalysts for industrial processes requiring high temperatures, spanning
biotechnology, biofuels, detergents, and more. Thermophilic lipase from Bacillus toyonensis and Bacillus
thuringiensis consortium was purified and characterized. Purification of lipases to homogeneity was
conducted by precipitation with ammonium sulphate, dialysis and chromatography (G-75 gel filtration) with
a final recovery of 27.09% with 39.27 fold purification. The molecular weight of Bacillus consortium was 41
kDa using SDS-PAGE. Maximum activity of extracellular lipase was observed at pH 7.8, and temperature of
70oC. Conclusively, the thermophilic bacterial consortium can be exploited for biotechnological applications
for production of lipase on large scale, where alkaline conditions prevailed.