Purification and characterization of thermo-alkaline stable lipase from Bacillus coagulans and its compatibility with commercially available detergents

Abstract

Thermo-alkaline stable lipase producing B. coagulans was isolated and identified by 16S rRNA sequencing. The lipase production was optimized using different growth parameters. The enzyme was purified and characterized in terms of pH, temperature, solvents, heavy metal ions and inhibitors. Compatibility with commercially available detergents was also studied. The isolate showed maximum lipase production at 37 ⁰C; pH of 9 within 48 h. Addition of magnesium chloride increased lipase production. Sephadex G-100 chromatography was used to purify lipase. The enzyme showed maximum activity at pH 8 of 30 ⁰C. Lipase form B. coagulans was active at a wide range of temperature between 30-70 ⁰C. It was stable in most of the solvents at a concentration 5 and 10%, except dimethyl sulfoxide (DMSO) and methanol. Iodoacetic acid (IAA) and p-chloromercuribenzoic acid (pCMB) had an inhibitory effect on lipase. The lipase was compatible with commercially available detergents that increased the brightness and whiteness of the tested cotton fabrics. Lipase from B. coagulans with alkaline stability at a wide range of temperature has potential application in the detergent industry.