“Production and Application Recombinant Lipase from Pichia pastoris”

Nithi Chalinthornwat, Thitiwat Bunket, Nisa Patikarnmonthon, and Chuenchit Boonchird

Lipase is an enzyme which can catalyse the hydrolysis of ester bond in lipid into fatty acid and glycerol. Lipase are available in several organisms, including animals, plants, and microorganisms. Lipase used in industrial applications are recombinant lipase synthesized by microorganisms according to its rapid production, high production yield and ease of manipulation. Recombinant lipase are mainly produced from both yeast Saccharomyces cerevisiae and Pichia pastoris, as they are GRAS microorganisms and also provide the high yield of protein. Lipase can be used in various applications, such as bioethanol production, wastewater treatment. Besides its hydrolysis activity, lipase can be used in transesterification, catalysis of exchange of alkyl group between alcohol and ester. This reaction can be used for modification of compound by attaching the fatty acid group onto the compound to enhance its hydrophobicity.

This work will focus on the application of recombinant lipase produced from thermotolerant yeast. The production condition of lipase will be optimized. The parameter which could affect the enzyme activity will be examined. Transesterification activity of this recombinant lipase will be investigated. Recombinant lipase with transesterification activity will be used in dextran modification as a model application in comparison with the commercially available enzyme.

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