Biocatalytic transesterification of algal oil employing a heterogenous methanol tolerant lipase enzyme aggregate from Bacillus mycoides strain CV18

[Display omitted] •Purification and characterisation of methanol tolerant lipase from Bacillus mycoides.•Algal lipid transesterification employing cross-linked lipase enzyme aggregate.•Analysis of algal biodiesel (FAME) by TLC and FTIR.•Comparative FTIR analysis of algal biodiesel, algal lipid, and petroleum. Methanol induced lipase inactivation is the major hindrance in commercialization of enzyme catalyzed biodiesel production. Thus, methanol tolerance is highly needed for the lipase to be used in transesterification reaction. Hence, by virtue of such desirability, a methanol tolerant, extracellular lipase FDS8(L) was extracted from Bacillus mycoides strain CV18 and purified to homogeneity with 22.3 % yield. It was a non-position specific, alkaline lipase with 44 kDa of relative molecular mass and had no isoforms (confirmed by zymography). It showed optimal activity at pH 9.0 and 30 °C temperature, while stability in the pH range 7.0–10.0 and temperature upto 50 °C. Organic solvents (hexane, acetone and methanol) as well as metal ions (Mg2+, Mn2+ and Na+) had stimulatory effects on lipase activity. Lipase immobilization was done using glutaraldehyde to form cross linked lipase enzyme aggregate (CLEA) which further enhanced its stability in the presence of methanol. Owing to its methanol tolerance property, it was employed heterogeneously for catalyzing transesterification of algal lipids in methanol. The qualitative efficacy of the FDS8 lipase in converting algal lipids into biodiesel was confirmed after analyzing the hexane extracted transesterification products by TLC and FTIR spectroscopy.