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Lipase-catalyzed dimethyl adipate synthesis: response surface modeling and kinetics


Chaibakhsh, Naz and Abdul Rahman, Mohd Basyaruddin and Basri, Mahiran and Salleh, Abu Bakar and Abd. Aziz, Suraini (2010) Lipase-catalyzed dimethyl adipate synthesis: response surface modeling and kinetics. Biotechnology Journal, 5 (8). pp. 848-855. ISSN 1860-6768; ESSN: 1860-7314


Dimethyl adipate (DMA) was synthesized by immobilized Candida antarctica lipase B-catalyzed esterification of adipic acid and methanol. To optimize the reaction conditions of ester production, response surface methodology was applied, and the effects of four factors namely, time, temperature, enzyme concentration, and molar ratio of substrates on product synthesis were determined. A statistical model predicted that the maximum conversion yield would be 97.6%, at the optimal conditions of 58.5°C, 54.0 mg enzyme, 358.0 min, and 12:1 molar ratio of methanol to adipic acid. The R2 (0.9769) shows a high correlation between predicted and experimental values. The kinetics of the reaction was also investigated in this study. The reaction was found to obey the ping-pong bi-bi mechanism with methanol inhibition. The kinetic parameters were determined and used to simulate the experimental results. A good quality of fit was observed between the simulated and experimental initial rates.

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Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
Faculty of Science
Institute of Bioscience
DOI Number: https://doi.org/10.1002/biot.201000063
Publisher: Wiley
Keywords: Biocatalysis; Enzymatic synthesis; Esterification; Kinetics; Optimization
Depositing User: Nurul Ainie Mokhtar
Date Deposited: 01 Aug 2015 00:57
Last Modified: 02 Nov 2015 03:17
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1002/biot.201000063
URI: http://psasir.upm.edu.my/id/eprint/15461
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