Lipase‐catalyzed dimethyl adipate synthesis: Response surface modeling and kinetics

Abstract 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, temperatur...

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Published in:Biotechnology Journal
Main Authors: Chaibakhsh, Naz, Rahman, Mohd Basyaruddin Abdul, Basri, Mahiran, Salleh, Abu Bakar, Abd‐Aziz, Suraini
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2010
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Online Access:http://dx.doi.org/10.1002/biot.201000063
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spelling crwiley:10.1002/biot.201000063 2024-09-09T19:09:31+00:00 Lipase‐catalyzed dimethyl adipate synthesis: Response surface modeling and kinetics Chaibakhsh, Naz Rahman, Mohd Basyaruddin Abdul Basri, Mahiran Salleh, Abu Bakar Abd‐Aziz, Suraini 2010 http://dx.doi.org/10.1002/biot.201000063 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbiot.201000063 https://onlinelibrary.wiley.com/doi/pdf/10.1002/biot.201000063 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biotechnology Journal volume 5, issue 8, page 848-855 ISSN 1860-6768 1860-7314 journal-article 2010 crwiley https://doi.org/10.1002/biot.201000063 2024-06-20T04:26:58Z Abstract 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 R 2 (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. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Biotechnology Journal 5 8 848 855
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description Abstract 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 R 2 (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.
format Article in Journal/Newspaper
author Chaibakhsh, Naz
Rahman, Mohd Basyaruddin Abdul
Basri, Mahiran
Salleh, Abu Bakar
Abd‐Aziz, Suraini
spellingShingle Chaibakhsh, Naz
Rahman, Mohd Basyaruddin Abdul
Basri, Mahiran
Salleh, Abu Bakar
Abd‐Aziz, Suraini
Lipase‐catalyzed dimethyl adipate synthesis: Response surface modeling and kinetics
author_facet Chaibakhsh, Naz
Rahman, Mohd Basyaruddin Abdul
Basri, Mahiran
Salleh, Abu Bakar
Abd‐Aziz, Suraini
author_sort Chaibakhsh, Naz
title Lipase‐catalyzed dimethyl adipate synthesis: Response surface modeling and kinetics
title_short 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_sort lipase‐catalyzed dimethyl adipate synthesis: response surface modeling and kinetics
publisher Wiley
publishDate 2010
url http://dx.doi.org/10.1002/biot.201000063
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbiot.201000063
https://onlinelibrary.wiley.com/doi/pdf/10.1002/biot.201000063
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Biotechnology Journal
volume 5, issue 8, page 848-855
ISSN 1860-6768 1860-7314
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1002/biot.201000063
container_title Biotechnology Journal
container_volume 5
container_issue 8
container_start_page 848
op_container_end_page 855
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