Thermal stability enhancement of Candida rugosa lipase using ionic liquids

The thermal stability of Candida rugosa (C. rugosa) lipase was investigated and compared in n-hexane, benzene, dibutylether as well as [bmim] PF6 and [omim] PF6 ionic liquids and the effect of solvent polarity and water activity were evaluated. Deactivation of the enzyme followed a series-type kinetic model. First order deactivation rate constants and the ratios of specific activities were determined and the kinetics of deactivation were studied. Among the organic solvents, the best stability was observed in n-hexane with a half-life of 6.5 h at water activity of 0.51. In ionic liquids, however, even longer half lives were obtained, and the enzyme was stable in these solvents at 50 degrees C. The highest half-life times were obtained in [bmim] PF6 (12.3 h) and [omim] PF6 (10.6 h). A direct correlation was found between solvent polarity and thermal stability since the higher the polarity of the solvent, the lower was the stability decrease at 50 degrees C comparing to that at 30 degrees C.