| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 70673 | Journal of Molecular Catalysis B: Enzymatic | 2011 | 10 Pages |
The Talaromyces thermophilus lipase (TTL) was immobilized by different methods namely adsorption, ionic binding and covalent coupling, using various carriers. Chitosan, pre-treated with glutaraldehyde, was selected as the most suitable support material preserving the catalytic activity almost intact and offering maximum immobilization capacity (76% and 91%, respectively). The chitosan-immobilized lipase could be reputably used for ten cycles with more than 80% of its initial hydrolytic activity. Shift in the optimal temperature from 50 to 60 °C and in the pH from 9.5 to 10, were observed for the immobilized lipase when compared to the free enzyme.The catalytic esterification of oleic acid with 1-butanol has been carried out using hexane as organic solvent. A high performance synthesis of 1-butyl oleate was obtained (95% of conversion yield) at 60 °C with a molar ratio of 1:1 oleic acid to butanol and using 100 U (0.2 g) of immobilized lipase. The esterification product is analysed by GC/MS to confirm the conversion percentage calculated by titration.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideResearch highlights▶ Chitosan, pre-treated with glutaraldehyde, was selected as the best support material for Talaromyces thermophilus lipase (TTL). ▶ A shift in the optimal temperature from 50 to 60 °C and in the pH from 9.5 to 10, were observed for the immobilized lipase when compared to the free enzyme. ▶ A high performance synthesis of 1-butyl oleate (analysed by GC/MS) was obtained at 95% of conversion yield.
