Immobilization of Organic Solvent-Tolerant Lipase from Pseudomonas mendocina M-37 with Potential Synthetic Activities

Abstract

A thermostable solvent-tolerant lipase was isolated from Pseudomonas mendocina M-37. The lipase production medium was optimized for cost-effective production. Olive oil as a carbon source, and glycine as a nitrogen source were selected as the best for maximum lipase production. Medium optimization led to 3.75-fold increase in the lipase production. The extracellular lipase was purified 42.2-fold to homogeneity by precipitation using polyethyleneglycol, ultrafiltration and hydrophobic interaction chromatography. Its molecular mass, determined with sodium dodecyl sulphate polyacrylamide gel electrophoresis, was 32 kDa. The enzyme was further immobilized on microcrystalline cellulose. The lipase showed an optimal water activity of 0.53 for both, acidolysis and interesterification reactions. Six- to sevenfold increase in synthetic activity of immobilized lipase was observed when interesterification activity of 0.139 IU/mg and transesterification activity of 0.181 IU/mg, respectively, were obtained. This is the first report on Pseudomonas mendocina lipase with synthetic activity immobilized on microcrystalline cellulose.

Keywords

• acidolysis
• immobilization
• organic solvent-tolerant lipase
• Pseudomonas mendocina
• purification