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

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...

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Main Authors: Chaibakhsh, Naz, Abdul Rahman, Mohd Basyaruddin, Basri, Mahiran, Salleh, Abu Bakar, Abd. Aziz, Suraini
Format: Article
Language:English
Published: Wiley 2010
Online Access:http://psasir.upm.edu.my/id/eprint/15461/1/Lipase-catalyzed%20dimethyl%20adipate%20synthesis%20response%20surface%20modeling%20and%20kinetics.pdf
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author Chaibakhsh, Naz
Abdul Rahman, Mohd Basyaruddin
Basri, Mahiran
Salleh, Abu Bakar
Abd. Aziz, Suraini
author_facet Chaibakhsh, Naz
Abdul Rahman, Mohd Basyaruddin
Basri, Mahiran
Salleh, Abu Bakar
Abd. Aziz, Suraini
author_sort Chaibakhsh, Naz
collection UPM
description 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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spelling upm.eprints-154612015-11-02T03:17:35Z http://psasir.upm.edu.my/id/eprint/15461/ Lipase-catalyzed dimethyl adipate synthesis: response surface modeling and kinetics Chaibakhsh, Naz Abdul Rahman, Mohd Basyaruddin Basri, Mahiran Salleh, Abu Bakar Abd. Aziz, Suraini 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. Wiley 2010-08 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/15461/1/Lipase-catalyzed%20dimethyl%20adipate%20synthesis%20response%20surface%20modeling%20and%20kinetics.pdf 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 10.1002/biot.201000063
spellingShingle Chaibakhsh, Naz
Abdul Rahman, Mohd Basyaruddin
Basri, Mahiran
Salleh, Abu Bakar
Abd. Aziz, Suraini
Lipase-catalyzed dimethyl adipate synthesis: response surface modeling and kinetics
title Lipase-catalyzed dimethyl adipate synthesis: response surface modeling and kinetics
title_full Lipase-catalyzed dimethyl adipate synthesis: response surface modeling and kinetics
title_fullStr Lipase-catalyzed dimethyl adipate synthesis: response surface modeling and kinetics
title_full_unstemmed Lipase-catalyzed dimethyl adipate synthesis: response surface modeling and kinetics
title_short Lipase-catalyzed dimethyl adipate synthesis: response surface modeling and kinetics
title_sort lipase catalyzed dimethyl adipate synthesis response surface modeling and kinetics
url http://psasir.upm.edu.my/id/eprint/15461/1/Lipase-catalyzed%20dimethyl%20adipate%20synthesis%20response%20surface%20modeling%20and%20kinetics.pdf
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