Effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase B from Candida antarctica
[Background] In this work two immobilized preparations of lipase (EC 3.1.1.3) B from Candida antarctica (CALB) were compared as biocatalysts in the synthesis of ethyl butyrate, a short‐chain esters with fruity notes. Commercial Novozym 435 and CALB immobilized on styrene‐divinylbenzene beads (MCI‐CA...
Published in: | Journal of Chemical Technology & Biotechnology |
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John Wiley & Sons
2013
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Online Access: | http://hdl.handle.net/10261/182705 https://doi.org/10.1002/jctb.3945 https://doi.org/10.13039/501100004837 https://doi.org/10.13039/501100003593 https://doi.org/10.13039/501100004263 |
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ftcsic:oai:digital.csic.es:10261/182705 2024-02-11T09:56:36+01:00 Effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase B from Candida antarctica Friedrich, John L. R. Peña, Fernanda P. García-Galán, Cristina Fernández-Lafuente, Roberto Ayub, Marco A. Z. Rodrigues, Rafael C. Fundação de Amparo à Pesquisa do Estado do Rio Grande do Sul Ministerio de Ciencia e Innovación (España) Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) 2013-06 http://hdl.handle.net/10261/182705 https://doi.org/10.1002/jctb.3945 https://doi.org/10.13039/501100004837 https://doi.org/10.13039/501100003593 https://doi.org/10.13039/501100004263 unknown John Wiley & Sons https://doi.org/10.1002/jctb.3945 Journal of Chemical Technology and Biotechnology 88(6): 1089-1095 (2013) 0268-2575 http://hdl.handle.net/10261/182705 doi:10.1002/jctb.3945 1097-4660 http://dx.doi.org/10.13039/501100004837 http://dx.doi.org/10.13039/501100003593 http://dx.doi.org/10.13039/501100004263 none Ethyl butyrate Enzyme reuse RSM Esterification CALB Flavour esters artículo http://purl.org/coar/resource_type/c_6501 2013 ftcsic https://doi.org/10.1002/jctb.394510.13039/50110000483710.13039/50110000359310.13039/501100004263 2024-01-16T10:39:40Z [Background] In this work two immobilized preparations of lipase (EC 3.1.1.3) B from Candida antarctica (CALB) were compared as biocatalysts in the synthesis of ethyl butyrate, a short‐chain esters with fruity notes. Commercial Novozym 435 and CALB immobilized on styrene‐divinylbenzene beads (MCI‐CALB) were tested for esterification reactions. Central composite design and response surface methodology were used to optimize the reaction temperature, substrate molar ratio, enzyme content, and the added water. [Results] The two enzymatic preparations presented different optimal conditions concerning ethyl butyrate production, with higher yields of conversion around 85% in 1.5 h being achieved. However, MCI‐CALB presented productivities 1.6 times higher than Novozym 435. The main difference between the biocatalysts was in relation to operational stability during batch reuse experiments, in which MCI‐CALB retained 80% of its initial activity after eight batches, while Novozym 435 retained only 20% under the same conditions. [Conclusion] It was verified that variations in the protocols for enzyme immobilization causes different optimal conditions for the esterification reaction. These are very interesting results because reaction times were short, producing high conversion yields and productivities considering the mass of biocatalyst used. This work was supported by grants from Fundação de Amparo a Pesquisa do Rio Grande do Sul (FAPERGS – ARD/2011) and CTQ2009‐07568 from Spanish Ministerio de Ciencia e Innovación. We also thank Ministerio de Ciencia e Innovación for a fellowship for C. Garcia‐Galan and Conselho Nacional de Desenvolvimento Científico Tecnológico (CNPq ‐ Brazil) for a fellowship to J. L. R. Friedrich. Peer Reviewed Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Journal of Chemical Technology & Biotechnology 88 6 1089 1095 |
institution |
Open Polar |
collection |
Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
unknown |
topic |
Ethyl butyrate Enzyme reuse RSM Esterification CALB Flavour esters |
spellingShingle |
Ethyl butyrate Enzyme reuse RSM Esterification CALB Flavour esters Friedrich, John L. R. Peña, Fernanda P. García-Galán, Cristina Fernández-Lafuente, Roberto Ayub, Marco A. Z. Rodrigues, Rafael C. Effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase B from Candida antarctica |
topic_facet |
Ethyl butyrate Enzyme reuse RSM Esterification CALB Flavour esters |
description |
[Background] In this work two immobilized preparations of lipase (EC 3.1.1.3) B from Candida antarctica (CALB) were compared as biocatalysts in the synthesis of ethyl butyrate, a short‐chain esters with fruity notes. Commercial Novozym 435 and CALB immobilized on styrene‐divinylbenzene beads (MCI‐CALB) were tested for esterification reactions. Central composite design and response surface methodology were used to optimize the reaction temperature, substrate molar ratio, enzyme content, and the added water. [Results] The two enzymatic preparations presented different optimal conditions concerning ethyl butyrate production, with higher yields of conversion around 85% in 1.5 h being achieved. However, MCI‐CALB presented productivities 1.6 times higher than Novozym 435. The main difference between the biocatalysts was in relation to operational stability during batch reuse experiments, in which MCI‐CALB retained 80% of its initial activity after eight batches, while Novozym 435 retained only 20% under the same conditions. [Conclusion] It was verified that variations in the protocols for enzyme immobilization causes different optimal conditions for the esterification reaction. These are very interesting results because reaction times were short, producing high conversion yields and productivities considering the mass of biocatalyst used. This work was supported by grants from Fundação de Amparo a Pesquisa do Rio Grande do Sul (FAPERGS – ARD/2011) and CTQ2009‐07568 from Spanish Ministerio de Ciencia e Innovación. We also thank Ministerio de Ciencia e Innovación for a fellowship for C. Garcia‐Galan and Conselho Nacional de Desenvolvimento Científico Tecnológico (CNPq ‐ Brazil) for a fellowship to J. L. R. Friedrich. Peer Reviewed |
author2 |
Fundação de Amparo à Pesquisa do Estado do Rio Grande do Sul Ministerio de Ciencia e Innovación (España) Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) |
format |
Article in Journal/Newspaper |
author |
Friedrich, John L. R. Peña, Fernanda P. García-Galán, Cristina Fernández-Lafuente, Roberto Ayub, Marco A. Z. Rodrigues, Rafael C. |
author_facet |
Friedrich, John L. R. Peña, Fernanda P. García-Galán, Cristina Fernández-Lafuente, Roberto Ayub, Marco A. Z. Rodrigues, Rafael C. |
author_sort |
Friedrich, John L. R. |
title |
Effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase B from Candida antarctica |
title_short |
Effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase B from Candida antarctica |
title_full |
Effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase B from Candida antarctica |
title_fullStr |
Effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase B from Candida antarctica |
title_full_unstemmed |
Effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase B from Candida antarctica |
title_sort |
effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase b from candida antarctica |
publisher |
John Wiley & Sons |
publishDate |
2013 |
url |
http://hdl.handle.net/10261/182705 https://doi.org/10.1002/jctb.3945 https://doi.org/10.13039/501100004837 https://doi.org/10.13039/501100003593 https://doi.org/10.13039/501100004263 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
https://doi.org/10.1002/jctb.3945 Journal of Chemical Technology and Biotechnology 88(6): 1089-1095 (2013) 0268-2575 http://hdl.handle.net/10261/182705 doi:10.1002/jctb.3945 1097-4660 http://dx.doi.org/10.13039/501100004837 http://dx.doi.org/10.13039/501100003593 http://dx.doi.org/10.13039/501100004263 |
op_rights |
none |
op_doi |
https://doi.org/10.1002/jctb.394510.13039/50110000483710.13039/50110000359310.13039/501100004263 |
container_title |
Journal of Chemical Technology & Biotechnology |
container_volume |
88 |
container_issue |
6 |
container_start_page |
1089 |
op_container_end_page |
1095 |
_version_ |
1790604444075819008 |