Abstract
Bacteria produced maximum thermolabile alkaline lipase at 25 degrees C after 96 h incubation in alkaline conditions. We tested the effect of different salts on its activity and found that CaCl2 stimulated activity by 3766 U, whereas, the ZnSO4 and FeCl3 strongly inhibited the activity. A novel organic solvent stable alkaliphilic lipase enzyme (GenBank: QBA82211) encoding from YLip gene (GenBank ID MH338242), was amplified from psychrotrophic Pseudomonas spp. The cloned YLip, expressed in BL21 (lambda DE3), gave a soluble protein of molecular mass 32-kDa after induction with 1 mM IPTG followed by standard purification procedures. It maintained thermal stability from 4 to 60 degrees C and half of the catalytic activity was inhibited subsequently after 60 min of incubation at 60 degrees C. Enhanced lipolytic activity of the lipase segregated from Pseudomonas spp. was observed in the presence of organic solvents of dimethyl sulfoxide (DMSO) and ethanol. Present results suggest that YLip as thermolabile lipase had comparatively maximum thermal stability and remarkable resistance toward organic solvents. Overall, this cold active alkaliphilic lipase is a potentially desirable candidate for biotechnological application, because of its stability at low temperature across a range of organic solvents. (C) 2019 Friends Science Publishers