doi:10.4061/2011/162987 Research Article Effect of Alcohol Structure on the Optimum Condition for
Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Immobilized Candida antarctica lipase B, Novozym 435, was used as the biocatalyst in the esterification of adipic acid with four different isomers of butan...
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ftciteseerx:oai:CiteSeerX.psu:10.1.1.271.2010 2023-05-15T14:01:57+02:00 doi:10.4061/2011/162987 Research Article Effect of Alcohol Structure on the Optimum Condition for Mohd Basyaruddin Abdul Rahman Naz Chaibakhsh Mahiran Basri The Pennsylvania State University CiteSeerX Archives 2011 application/zip http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.271.2010 en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.271.2010 Metadata may be used without restrictions as long as the oai identifier remains attached to it. ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/4f/e0/Biotechnol_Res_Int_2011_Dec_27_2011_162987.tar.gz text 2011 ftciteseerx 2016-01-07T20:39:02Z Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. 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. 1. Text Antarc* Antarctica Unknown |
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Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. 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. 1. |
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The Pennsylvania State University CiteSeerX Archives |
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Text |
author |
Mohd Basyaruddin Abdul Rahman Naz Chaibakhsh Mahiran Basri |
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Mohd Basyaruddin Abdul Rahman Naz Chaibakhsh Mahiran Basri doi:10.4061/2011/162987 Research Article Effect of Alcohol Structure on the Optimum Condition for |
author_facet |
Mohd Basyaruddin Abdul Rahman Naz Chaibakhsh Mahiran Basri |
author_sort |
Mohd Basyaruddin |
title |
doi:10.4061/2011/162987 Research Article Effect of Alcohol Structure on the Optimum Condition for |
title_short |
doi:10.4061/2011/162987 Research Article Effect of Alcohol Structure on the Optimum Condition for |
title_full |
doi:10.4061/2011/162987 Research Article Effect of Alcohol Structure on the Optimum Condition for |
title_fullStr |
doi:10.4061/2011/162987 Research Article Effect of Alcohol Structure on the Optimum Condition for |
title_full_unstemmed |
doi:10.4061/2011/162987 Research Article Effect of Alcohol Structure on the Optimum Condition for |
title_sort |
doi:10.4061/2011/162987 research article effect of alcohol structure on the optimum condition for |
publishDate |
2011 |
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http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.271.2010 |
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Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/4f/e0/Biotechnol_Res_Int_2011_Dec_27_2011_162987.tar.gz |
op_relation |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.271.2010 |
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Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
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1766272016284909568 |