期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 68, 期 3-4, 页码 230-239出版社
ELSEVIER
DOI: 10.1016/j.molcatb.2010.11.010
关键词
Talaromyces thermophilus lipase; Immobilization; Chitosan; Esterification
资金
- Ministere de l'Enseignement Superieur de la Recherche Sientifique et de la Technologie, Tunisia
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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