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Selective production of 1-monocaprin by porcine liver carboxylesterase-catalyzed esterification: Its enzyme kinetics and catalytic performance

Paper ID Volume ID Publish Year Pages File Format Full-Text
16895 42621 2016 7 PDF Available
Title
Selective production of 1-monocaprin by porcine liver carboxylesterase-catalyzed esterification: Its enzyme kinetics and catalytic performance
Abstract

•Porcine liver esterase has regio-selectivity for the synthesis of 1-monocarpin.•PLE-esterification was achieved in the reverse micelles with AOT and isooctane.•R- and G/F-values were main factors for the conversion yield of PLE-esterification.•Apparent catalytic parameters of PLE-esterification were determined from kinetics.

Porcine liver carboxylesterase (PLE) belongs to carboxylesterase family (EC 3.1.1.1) as a serine-type esterase. The PLE-catalyzed esterification of capric acid with glycerol in reverse micelles was investigated on the catalytic performance and enzyme kinetics. The most suitable structure of reverse micelles was comprised of isooctane (reaction medium) and bis(2-ethylhexyl) sodium sulfosuccinate (AOT, anionic surfactant) with 0.1 of R-value ([water]/[surfactant]) and 3.0 of G/F-value ([glycerol]/[fatty acid]) for the PLE-catalyzed esterification. In the aspect of regio-selectivity, the PLE mainly produced 1-monocaprin without any other products (di- and/or tricaprins of subsequent reactions). Furthermore, the degree of esterification at equilibrium state (after 4 h from the initiation) was 62.7% under the optimum conditions at pH 7.0 and 60 °C. Based on Hanes–Woolf plot, the apparent Km and Vmax values were calculated to be 16.44 mM and 38.91 μM/min/mg protein, respectively.

Keywords
Porcine liver carboxylesterase; Esterification; Reverse micelles; 1-monocaprin; Enzyme kinetics
First Page Preview
Selective production of 1-monocaprin by porcine liver carboxylesterase-catalyzed esterification: Its enzyme kinetics and catalytic performance
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 82, January 2016, Pages 51–57
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering