Partial purification and characterization of lipase from Geobacillus stearothermophilus AH22

The lipase was partially purified by ion exchange chromatography and gel filtration column chromatography, and was characterized from Geobacillus stearothermophilus AH22 strain. The lipase was purified 18.3-folds with 19.7% recovery. The lipase activity was determined by using p-nitrophenyl esters (C-2-C-12) as substrates. The K-m values of the enzyme for these substrates were found as 0.16, 0.02, 0.19 and 0.55mM, respectively, while V-max values were 0.52, 1.03, 0.72 and 0.15 Umg(-1). The enzyme showed maximum activity at 50 degrees C and between pH 8.0 and 9.0. The enzyme was found to be quite stable at pH range of 4.0-10.0, and thermal stability between 50 and 60 degrees C. It was found that the best inhibitory effect of the enzyme activity was of Hg2+. The inhibitory effect as orlistat, catechin, propyl paraben, p-coumaric acid, 3,4-dihydroxy hydro-cinnamic acid was examined. These results suggest that G. stearothermophilus AH22 lipase presents very suitable properties for industrial applications.