Optimization of synthesis of fatty acid methyl esters catalyzed by lipase B from Candida antarctica immobilized on hydrophobic supports
In this work two immobilized preparations of lipase (EC 3.1.1.3) B from Candida antarctica (CALB) were compared for the synthesis of fatty acid methyl esters (FAME) using soybean oil. Commercial Novozym 435 (CALB-435) and CALB immobilized on styrene-divinylbenzene beads (CALB–MCI) were tested for th...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
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Online Access: | http://hdl.handle.net/10261/182260 https://doi.org/10.1016/j.molcatb.2013.05.010 https://doi.org/10.13039/501100002322 https://doi.org/10.13039/501100004837 |
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ftcsic:oai:digital.csic.es:10261/182260 2024-02-11T09:56:40+01:00 Optimization of synthesis of fatty acid methyl esters catalyzed by lipase B from Candida antarctica immobilized on hydrophobic supports Poppe, Jakeline K. García-Galán, Cristina Matte, Carla R. Fernández-Lafuente, Roberto Rodrigues, Rafael C. Ayub, Marco A. Z. Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) Ministerio de Ciencia e Innovación (España) 2013-10 http://hdl.handle.net/10261/182260 https://doi.org/10.1016/j.molcatb.2013.05.010 https://doi.org/10.13039/501100002322 https://doi.org/10.13039/501100004837 unknown Elsevier https://doi.org/10.1016/j.molcatb.2013.05.010 Sí Journal of Molecular Catalysis - B Enzymatic 94: 51-56 (2013) 1381-1177 http://hdl.handle.net/10261/182260 doi:10.1016/j.molcatb.2013.05.010 1873-3158 http://dx.doi.org/10.13039/501100002322 http://dx.doi.org/10.13039/501100004837 none RSM Enzyme reuse Fatty acid methyl esters CALB Transesterification artículo http://purl.org/coar/resource_type/c_6501 2013 ftcsic https://doi.org/10.1016/j.molcatb.2013.05.01010.13039/50110000232210.13039/501100004837 2024-01-16T10:39:28Z In this work two immobilized preparations of lipase (EC 3.1.1.3) B from Candida antarctica (CALB) were compared for the synthesis of fatty acid methyl esters (FAME) using soybean oil. Commercial Novozym 435 (CALB-435) and CALB immobilized on styrene-divinylbenzene beads (CALB–MCI) were tested for the transesterification reactions. Central composite design (CCD) and response surface methodology (RSM) were used to optimize the reaction parameters, substrate molar ratio, enzyme content, and the added amount of water, on the initial reaction rate as response. The biocatalysts showed different optimal conditions for the production of FAME. For CALB-435, optima conditions were 5.6:1 molar ratio methanol:oil, 25% enzyme, and 5.44% of added water, while for MCI–CALB, these optima were 3:1 molar ratio methanol:oil, 25% enzyme, and 1.18% of added water, resulting in initial reaction rates of 51.47 mmol L−1 h−1, and 57 mmol L−1 h−1 of FAME, respectively. Conversions of 93.38% using CALB-435, and 99.03% using CALB–MCI were obtained after 72 h of reaction under the optimized conditions. Repeated batches of reaction were carried out to test the operational stability of biocatalysts, with both preparations keeping around 70% of their initial activity after eight batches. This work was supported by grants from Brazilian Coordenação de Aperfoiçoamento de Pessoal de Nível Superior (CAPES) and CTQ2009-07568 from Spanish Ministerio de Ciencia e Innovación. Peer Reviewed Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Journal of Molecular Catalysis B: Enzymatic 94 51 56 |
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Open Polar |
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Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
unknown |
topic |
RSM Enzyme reuse Fatty acid methyl esters CALB Transesterification |
spellingShingle |
RSM Enzyme reuse Fatty acid methyl esters CALB Transesterification Poppe, Jakeline K. García-Galán, Cristina Matte, Carla R. Fernández-Lafuente, Roberto Rodrigues, Rafael C. Ayub, Marco A. Z. Optimization of synthesis of fatty acid methyl esters catalyzed by lipase B from Candida antarctica immobilized on hydrophobic supports |
topic_facet |
RSM Enzyme reuse Fatty acid methyl esters CALB Transesterification |
description |
In this work two immobilized preparations of lipase (EC 3.1.1.3) B from Candida antarctica (CALB) were compared for the synthesis of fatty acid methyl esters (FAME) using soybean oil. Commercial Novozym 435 (CALB-435) and CALB immobilized on styrene-divinylbenzene beads (CALB–MCI) were tested for the transesterification reactions. Central composite design (CCD) and response surface methodology (RSM) were used to optimize the reaction parameters, substrate molar ratio, enzyme content, and the added amount of water, on the initial reaction rate as response. The biocatalysts showed different optimal conditions for the production of FAME. For CALB-435, optima conditions were 5.6:1 molar ratio methanol:oil, 25% enzyme, and 5.44% of added water, while for MCI–CALB, these optima were 3:1 molar ratio methanol:oil, 25% enzyme, and 1.18% of added water, resulting in initial reaction rates of 51.47 mmol L−1 h−1, and 57 mmol L−1 h−1 of FAME, respectively. Conversions of 93.38% using CALB-435, and 99.03% using CALB–MCI were obtained after 72 h of reaction under the optimized conditions. Repeated batches of reaction were carried out to test the operational stability of biocatalysts, with both preparations keeping around 70% of their initial activity after eight batches. This work was supported by grants from Brazilian Coordenação de Aperfoiçoamento de Pessoal de Nível Superior (CAPES) and CTQ2009-07568 from Spanish Ministerio de Ciencia e Innovación. Peer Reviewed |
author2 |
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) Ministerio de Ciencia e Innovación (España) |
format |
Article in Journal/Newspaper |
author |
Poppe, Jakeline K. García-Galán, Cristina Matte, Carla R. Fernández-Lafuente, Roberto Rodrigues, Rafael C. Ayub, Marco A. Z. |
author_facet |
Poppe, Jakeline K. García-Galán, Cristina Matte, Carla R. Fernández-Lafuente, Roberto Rodrigues, Rafael C. Ayub, Marco A. Z. |
author_sort |
Poppe, Jakeline K. |
title |
Optimization of synthesis of fatty acid methyl esters catalyzed by lipase B from Candida antarctica immobilized on hydrophobic supports |
title_short |
Optimization of synthesis of fatty acid methyl esters catalyzed by lipase B from Candida antarctica immobilized on hydrophobic supports |
title_full |
Optimization of synthesis of fatty acid methyl esters catalyzed by lipase B from Candida antarctica immobilized on hydrophobic supports |
title_fullStr |
Optimization of synthesis of fatty acid methyl esters catalyzed by lipase B from Candida antarctica immobilized on hydrophobic supports |
title_full_unstemmed |
Optimization of synthesis of fatty acid methyl esters catalyzed by lipase B from Candida antarctica immobilized on hydrophobic supports |
title_sort |
optimization of synthesis of fatty acid methyl esters catalyzed by lipase b from candida antarctica immobilized on hydrophobic supports |
publisher |
Elsevier |
publishDate |
2013 |
url |
http://hdl.handle.net/10261/182260 https://doi.org/10.1016/j.molcatb.2013.05.010 https://doi.org/10.13039/501100002322 https://doi.org/10.13039/501100004837 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
https://doi.org/10.1016/j.molcatb.2013.05.010 Sí Journal of Molecular Catalysis - B Enzymatic 94: 51-56 (2013) 1381-1177 http://hdl.handle.net/10261/182260 doi:10.1016/j.molcatb.2013.05.010 1873-3158 http://dx.doi.org/10.13039/501100002322 http://dx.doi.org/10.13039/501100004837 |
op_rights |
none |
op_doi |
https://doi.org/10.1016/j.molcatb.2013.05.01010.13039/50110000232210.13039/501100004837 |
container_title |
Journal of Molecular Catalysis B: Enzymatic |
container_volume |
94 |
container_start_page |
51 |
op_container_end_page |
56 |
_version_ |
1790604964990550016 |