Harnessing a thermo-active and alkaline lipase from novel strain of Brevibacillus borstelensis gp-1, for application in biodiesel synthesis

A novel thermo-active and alkaliphilic strain of Gp-1, isolated from hot water springs of Ganeshpuri, Maharashtra, India, identified as Brevibacillus borstelensis based on 16SrDNA characterization, with accession no. MT292327, at NCBI database. Statistical optimization of lipase production was done using Plackett-Burman algorithm and response surface methodology. Fermentative production of Gp-1 lipase was followed by partial purification, with 24.10 fold purification. Gp-1 lipase has molecular mass of 31 kDa, as determined by SDS-PAGE. Gp-1 lipase exhibited maximal specific activity at pH 10 and 55 degrees C, with stability up to 70 degrees C. Kinetic parameters analysis revealed Gp-1 lipase has K-m and V-max values of 1.544 mM and 31.25 mu M/mg. min, and specificity constant of 281.13 sec-1, with pNP caprylate as the base suited substrate. Gp-1 lipase was found to be retain more than 90% activity in presence of various organic solvents, and various commercial detergent formulations. The Gp-1 lipase was also tested for transesterification reactions, which revealed successful transesterification of coconut oil, olive oil and waste cooking oil, and conversion in esters. Hence, Gp-1 lipase stands out as a prospective candidate in biodiesel synthesis, a green energy alternative.