Effect of alcohol structure on the optimum condition for Novozym 435-catalyzed synthesis of adipate esters
Immobilized Candida antarctica lipase B, Novozym 435, was used as the biocatalyst in the esterification of adipic acid with four different isomers of butanol (n-butanol, sec-butanol, iso-butanol, and tert-butanol). Optimum conditions for the synthesis of adipate esters were obtained using response s...
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| Format: | Article |
| Language: | English |
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Hindawi Publishing Corporation
2011
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| Online Access: | http://psasir.upm.edu.my/id/eprint/25184/ http://psasir.upm.edu.my/id/eprint/25184/1/25184.pdf |
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| author | Abdul Rahman, Mohd Basyaruddin Chaibakhsh, Naz Basri, Mahiran |
| author_facet | Abdul Rahman, Mohd Basyaruddin Chaibakhsh, Naz Basri, Mahiran |
| author_sort | Abdul Rahman, Mohd Basyaruddin |
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| collection | Online Access |
| description | Immobilized Candida antarctica lipase B, Novozym 435, was used as the biocatalyst in the esterification of adipic acid with four different isomers of butanol (n-butanol, sec-butanol, iso-butanol, and tert-butanol). Optimum conditions for the synthesis of adipate esters were obtained using response surface methodology approach with a four-factor-five-level central composite design concerning important reaction parameters which include time, temperature, substrate molar ratio, and amount of enzyme. Reactions under optimized conditions has yielded a high percentage of esterification (>96%) for n-butanol, iso-butanol, and sec-butanol, indicating that extent of esterification is independent of the alcohol structure for primary and secondary alcohols at the optimum conditions. Minimum reaction time (135 min) for achieving maximum ester yield was obtained for iso-butanol. The required time for attaining maximum yield and also the initial rates in the synthesis of di-n-butyl and di-sec-butyl adipate were nearly the same. Immobilized Candida antarctica lipase B was also capable of esterifying tert-butanol with a maximum yield of 39.1%. The enzyme is highly efficient biocatalyst for the synthesis of adipate esters by offering a simple production process and a high esterification yield. |
| first_indexed | 2025-11-15T08:43:40Z |
| format | Article |
| id | upm-25184 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T08:43:40Z |
| publishDate | 2011 |
| publisher | Hindawi Publishing Corporation |
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| spelling | upm-251842017-11-01T09:42:10Z http://psasir.upm.edu.my/id/eprint/25184/ Effect of alcohol structure on the optimum condition for Novozym 435-catalyzed synthesis of adipate esters Abdul Rahman, Mohd Basyaruddin Chaibakhsh, Naz Basri, Mahiran Immobilized Candida antarctica lipase B, Novozym 435, was used as the biocatalyst in the esterification of adipic acid with four different isomers of butanol (n-butanol, sec-butanol, iso-butanol, and tert-butanol). Optimum conditions for the synthesis of adipate esters were obtained using response surface methodology approach with a four-factor-five-level central composite design concerning important reaction parameters which include time, temperature, substrate molar ratio, and amount of enzyme. Reactions under optimized conditions has yielded a high percentage of esterification (>96%) for n-butanol, iso-butanol, and sec-butanol, indicating that extent of esterification is independent of the alcohol structure for primary and secondary alcohols at the optimum conditions. Minimum reaction time (135 min) for achieving maximum ester yield was obtained for iso-butanol. The required time for attaining maximum yield and also the initial rates in the synthesis of di-n-butyl and di-sec-butyl adipate were nearly the same. Immobilized Candida antarctica lipase B was also capable of esterifying tert-butanol with a maximum yield of 39.1%. The enzyme is highly efficient biocatalyst for the synthesis of adipate esters by offering a simple production process and a high esterification yield. Hindawi Publishing Corporation 2011 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/25184/1/25184.pdf Abdul Rahman, Mohd Basyaruddin and Chaibakhsh, Naz and Basri, Mahiran (2011) Effect of alcohol structure on the optimum condition for Novozym 435-catalyzed synthesis of adipate esters. Biotechnology Research International, 2011. art. no. 162987. pp. 1-7. ISSN 2090-3138; ESSN: 2090-3146 https://www.hindawi.com/journals/btri/2011/162987/abs/ 10.4061/2011/162987 |
| spellingShingle | Abdul Rahman, Mohd Basyaruddin Chaibakhsh, Naz Basri, Mahiran Effect of alcohol structure on the optimum condition for Novozym 435-catalyzed synthesis of adipate esters |
| title | Effect of alcohol structure on the optimum condition for Novozym 435-catalyzed synthesis of adipate esters |
| title_full | Effect of alcohol structure on the optimum condition for Novozym 435-catalyzed synthesis of adipate esters |
| title_fullStr | Effect of alcohol structure on the optimum condition for Novozym 435-catalyzed synthesis of adipate esters |
| title_full_unstemmed | Effect of alcohol structure on the optimum condition for Novozym 435-catalyzed synthesis of adipate esters |
| title_short | Effect of alcohol structure on the optimum condition for Novozym 435-catalyzed synthesis of adipate esters |
| title_sort | effect of alcohol structure on the optimum condition for novozym 435-catalyzed synthesis of adipate esters |
| url | http://psasir.upm.edu.my/id/eprint/25184/ http://psasir.upm.edu.my/id/eprint/25184/ http://psasir.upm.edu.my/id/eprint/25184/ http://psasir.upm.edu.my/id/eprint/25184/1/25184.pdf |