Regular articleDevelopment of sucrose-complexed lipase to improve its transesterification activity and stability in organic solvents

- A commercial lipase was complexed with sucrose by freeze-dry.
- Buffer and concentration of sucrose for complexation was optimized.
- The complexed lipase showed a higher activity in some organic solvents.
- The complexed lipase kept higher proportion of its activity in some organic solvents.

A commercial lipase from Pseudomonas fluorescens was complexed with sucrose by freeze-drying to make the microenvironment around the lipase more hydrophilic in organic solvents, and then the stability and transesterification activity of sucrose-complexed lipases in organic solvents was examined. A lipase solution with 5 mM Tris-HCl buffer (pH 9.0) containing 1% (w/v) sucrose was found to be optimal for preparation of the sucrose-complexed lipase by freeze-drying. By complexed with sucrose, not only the lipase retains a higher proportion of its activity after incubation in 100% of n-decane, n-hexane, 1-octanol, 1-pentanol, or 1-propanol at 30 °C for 24 h, but the lipase also showed a higher transesterification activity in 100% (v/v) n-hexane and n-hexane containing 50% (v/v) of n-octane, 1-octanol, 1-pentanol, 1-propanol, or acetone. Using the simple and easy-to-use procedure, the sucrose-complexed lipase which can retain its activity in organic solvents was obtained.

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