An Investigation into the Factors Influencing Lipase-Catalyzed Intramolecular Lactonization Microaqueous Systems

Robinson, Gary K. and Alston, Mark J. and Knowles, C.J. and Cheetham, P.S.J. and Motion, K.R. (1994) An Investigation into the Factors Influencing Lipase-Catalyzed Intramolecular Lactonization Microaqueous Systems. Enzyme and Microbial Technology, 16 (10). pp. 855-863. ISSN 0141-0229. (The full text of this publication is not available from this repository)

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Abstract

Factors affecting the enzymatic intramolecular lactonization of 16-hydroxyhexadecanoic acid are presented. A screen of 33 enzymes, predominantly lipases, showed chat only a proportion were able to catalyze the synthetic reaction in a microaqueous environment Certain of these enzymes showed no observable formation of the oligolactones by the favored intermolecular esterification reaction, as reported by other workers. Indeed, the immobilized lipase from Candida antarctica showed formation of the intramolecular monolactone product, hexadecanolide, which could be produced continuously for 55 hs. Many variables were considered, including the choice of enzyme (source and preformulation), substrate concentration, product concentration solvent, temperature, pH, and water content of the system. The effect of these variables on hexadecanolide yield was analyzed statistically using a Plackett-Burman matrix. Significant effects were only demonstrated for the product hexadecanolide (stimulatory) and the substrate 16-hydroxyhexadecanoic acid (inhibitory).

Item Type: Article
Uncontrolled keywords: LIPASE; 16-HYDROXYHEXADECANOIC ACID; HEXADECANOLIDE; MICROAQUEOUS SYSTEM
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: P. Ogbuji
Date Deposited: 19 Jun 2009 14:44
Last Modified: 11 Apr 2014 11:12
Resource URI: http://kar.kent.ac.uk/id/eprint/20000 (The current URI for this page, for reference purposes)
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