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Porcine pancreas lipase catalysed acetylation of β-cyclodextrin anchored 4-t –butylcyclohexanol

Manohar, Balaraman and Divakar, S. (2004) Porcine pancreas lipase catalysed acetylation of β-cyclodextrin anchored 4-t –butylcyclohexanol. Indian Journal of Chemistry, 43B. pp. 2661-2665.

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Abstract

<p align="justify">Porcine pancreas lipase (PPL) catalyzed acetylation of 4-t-butylcyclohexanol gives less than 10% ester. However, when the latter is included inside hepatakis (2,3,6-tri-O-acetyl)-ß-cyclodextrin (ß -CD acetate) cavity, this enzymatic reaction affords the highest yield of 86.6%. The enzymatic esterification has been studied as a function of ß -CD acetate, PPL and acetic anhydride concentrations. A stoichiometry of 2: 1 for 4-t-butylcyclohexanol- ß -CD acetate complex is determined. Both trans and cis 4-t-butylcyclohexanol have been found to be acetylated. Gas chromatographic analysis of the reaction mixtures shows that trans/cis ratios of the esters formed varied from 2.1 to 4.34.</p>

Item Type: Article
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
Divisions: Food Engineering
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 08 Jun 2005
Last Modified: 22 Dec 2016 12:30
URI: http://ir.cftri.com/id/eprint/53

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