| Abstract: | Crude porcine pancreatic lipase was purified by removing water-insoluble impurities (residual lipid material) associated with it by a conventional method, using hydrotropic additives and by liquid coacervate extraction. Maximum yield with good recovery of activity was obtained when hydrotropes were used to separate the associated lipids from lipase. The thermostability of the enzyme was also checked in the solutions of additives such as sodium butyl monoglycol sulfate (Na-BMGS), proline and Triton X-114. In Na-BMGS solutions above a concentration of 0·2 mol dm−3 the lipase activity decreased beyond 50°C whereas in 1 mol dm−3 proline solution it was retained even at 80°C, showing a good thermostabilizing effect. However, in the presence of Triton X-114 the enzyme was completely inactivated with increase in temperature. © 1998 SCI. |
