Effect of salts on activity, stability and enantioselectivity of Candida rugosa lipase in isooctane

The effect of salts on activity and stability and enantioselectivity of Candida rugosa lipase in isooctane was studied. The activity of the lipase lyophilized with LiCl, NaCl or KCl and native lipase for the esterification of lauric acid with 1-propanol in isooctane at aw = 0.33 was 0.057, 0.044, 0.033 and 0.027 g g−1 min−1, respectively. The water content played a main role on the effect of lipase activity and lyophilization process did not change the conformation of the lipase. Salt incorporation could keep the conformation of the lipase and prevented the large change of optimum pH condition happening. The stability of the lyophilized lipase was 3.4 times as much as that of native lipase and the lipase thermostability was also improved. The enantioselectivity of lyophilized lipase (20.3) was about 1.6 times as much as that of the native lipase (13.0).