Exploration And Biochemical Characterization Of A Novel Lipase From Wrightia Tinctoria Latex

Abstract

Plant derived Lipase (triacylglycerol acyl hydrolase, EC 3.1.1.3.), has attracted a lot of attention in recently due to its ease of preparation, cost-efficiency and diverse biotechnological applications. In the present investigation, the novel lipase source from latex of Wrightia tinctoria (WTL) was studied. Their activities on p-nitrophenyl palmitate were optimal at pH 8.0 and 40 ◦C. Moreover, the activities of the lipases were inhibited by ethylenediaminetetraacetic acid, phenyl methyl-sulfonyl fluoride, and 4-(2-aminoethyl) benzene sulfonyl fluoride, and were reactivated by Ca2+ and Mg2+, indicating that both lipases are metalloenzymes and serine-type enzymes. Similarly, the influence of organic solvents like acetonitrile, methanol, isopropanol, ethanol acetone, and DMSO) and emulsifier agents (PEG 6000, Triton X100, SDS, CTAB Tween-20) were analysed. WTL maintained above 80% of its initial activity at a wide range of temperatures (20-70 °C) and   pH values (6-11), with an optimal temperature of 40°C and optimal pH at 9.0 with p-nitrophenyl palmitate as a substrate.   In addition, the kinetic models, Michaelis− Menten and Hill kinetic model were suggested. The obtained results were compared, and found Hill kinetic model describes better experimental compared to Michaelis− Menten model system. Our finding further insights, WTL would be suggested an excellent novel lipase candidate for industrial and biotechnological applications.