Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 68, Issue 3-4, Pages 230-239Publisher
ELSEVIER
DOI: 10.1016/j.molcatb.2010.11.010
Keywords
Talaromyces thermophilus lipase; Immobilization; Chitosan; Esterification
Funding
- Ministere de l'Enseignement Superieur de la Recherche Sientifique et de la Technologie, Tunisia
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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 degrees 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 degrees 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. (C) 2010 Elsevier B.V. All rights reserved.
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