Biochemical characterisation of lipase from a new strain of bacillus sp. ITP-001

Abstract

Lipases are characterised mainly by catalytic versatility and application in different industrial segments. The aim of this study was to biochemically characterise a lipase from a new strain of Bacillus sp. ITP-001. The isoelectric point and molecular mass were 3.12 and 54 kDa, respectively. The optima lipase activity was 276 U g-1 at pH 7.0 and a temperature of 80°C, showing greater stability at pH 5.0 and 37°C. Enzymatic activity was stimulated by various ions and pyridine, and inhibited by Cu+ and ethanol. The values of Km and vmax were 105.26 mmol and 0.116 mmol min-1 g-1, respectively determined by the Eadie-Scatchard method.