Enzymatic synthesis of triacylglycerols of docosahexaenoic acid: Transesterification of its ethyl esters with glycerol
The synthesis of docosahexaenoyl triacylglycerides at low temperature (e.g., 50°C) using biocatalysts of 6 commercial lipases adsorbed on hydrophobic supports was studied. In general, the triacylglyceride yields were very low with the exceptions of those produced with the enzymes from Candida antarc...
Published in: | Food Chemistry |
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Online Access: | http://hdl.handle.net/10261/149838 https://doi.org/10.1016/j.foodchem.2015.04.095 |
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ftcsic:oai:digital.csic.es:10261/149838 2024-02-11T09:57:08+01:00 Enzymatic synthesis of triacylglycerols of docosahexaenoic acid: Transesterification of its ethyl esters with glycerol Moreno-Pérez, Sonia Luna, Pilar Señoráns, Francisco J. Guisán, José Manuel Fernández-Lorente, Gloria 2015 http://hdl.handle.net/10261/149838 https://doi.org/10.1016/j.foodchem.2015.04.095 unknown Elsevier Sí doi:10.1016/j.foodchem.2015.04.095 issn: 0308-8146 Food Chemistry 187: 225-229 (2015) http://hdl.handle.net/10261/149838 none Lipases adsorbed on hydrophobic supports Transesterification by immobilized lipases Synthesis of tri-DHA artículo http://purl.org/coar/resource_type/c_6501 2015 ftcsic https://doi.org/10.1016/j.foodchem.2015.04.095 2024-01-16T10:23:13Z The synthesis of docosahexaenoyl triacylglycerides at low temperature (e.g., 50°C) using biocatalysts of 6 commercial lipases adsorbed on hydrophobic supports was studied. In general, the triacylglyceride yields were very low with the exceptions of those produced with the enzymes from Candida antarctica fraction B, CALB (82%), and those produced with the enzyme from Pseudomonas fluorescens, PFL (57%). The reactions were performed under vacuum to remove the released ethanol. The yields varied widely when different derivatives of CALB were used, and they were higher when CALB adsorbed on hydrophobic supports was used (82%). One interesting by-product (18% of sn-2 monoacylglyceride of DHA) remained at the end of the synthetic process. CALB adsorbed on Sepabeads exhibited better activity and stability than did the commercial derivative Novozym 435. The best CALB biocatalyst preserved 90% of the activity after 30 days under the reaction conditions. Peer Reviewed Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Food Chemistry 187 225 229 |
institution |
Open Polar |
collection |
Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
unknown |
topic |
Lipases adsorbed on hydrophobic supports Transesterification by immobilized lipases Synthesis of tri-DHA |
spellingShingle |
Lipases adsorbed on hydrophobic supports Transesterification by immobilized lipases Synthesis of tri-DHA Moreno-Pérez, Sonia Luna, Pilar Señoráns, Francisco J. Guisán, José Manuel Fernández-Lorente, Gloria Enzymatic synthesis of triacylglycerols of docosahexaenoic acid: Transesterification of its ethyl esters with glycerol |
topic_facet |
Lipases adsorbed on hydrophobic supports Transesterification by immobilized lipases Synthesis of tri-DHA |
description |
The synthesis of docosahexaenoyl triacylglycerides at low temperature (e.g., 50°C) using biocatalysts of 6 commercial lipases adsorbed on hydrophobic supports was studied. In general, the triacylglyceride yields were very low with the exceptions of those produced with the enzymes from Candida antarctica fraction B, CALB (82%), and those produced with the enzyme from Pseudomonas fluorescens, PFL (57%). The reactions were performed under vacuum to remove the released ethanol. The yields varied widely when different derivatives of CALB were used, and they were higher when CALB adsorbed on hydrophobic supports was used (82%). One interesting by-product (18% of sn-2 monoacylglyceride of DHA) remained at the end of the synthetic process. CALB adsorbed on Sepabeads exhibited better activity and stability than did the commercial derivative Novozym 435. The best CALB biocatalyst preserved 90% of the activity after 30 days under the reaction conditions. Peer Reviewed |
format |
Article in Journal/Newspaper |
author |
Moreno-Pérez, Sonia Luna, Pilar Señoráns, Francisco J. Guisán, José Manuel Fernández-Lorente, Gloria |
author_facet |
Moreno-Pérez, Sonia Luna, Pilar Señoráns, Francisco J. Guisán, José Manuel Fernández-Lorente, Gloria |
author_sort |
Moreno-Pérez, Sonia |
title |
Enzymatic synthesis of triacylglycerols of docosahexaenoic acid: Transesterification of its ethyl esters with glycerol |
title_short |
Enzymatic synthesis of triacylglycerols of docosahexaenoic acid: Transesterification of its ethyl esters with glycerol |
title_full |
Enzymatic synthesis of triacylglycerols of docosahexaenoic acid: Transesterification of its ethyl esters with glycerol |
title_fullStr |
Enzymatic synthesis of triacylglycerols of docosahexaenoic acid: Transesterification of its ethyl esters with glycerol |
title_full_unstemmed |
Enzymatic synthesis of triacylglycerols of docosahexaenoic acid: Transesterification of its ethyl esters with glycerol |
title_sort |
enzymatic synthesis of triacylglycerols of docosahexaenoic acid: transesterification of its ethyl esters with glycerol |
publisher |
Elsevier |
publishDate |
2015 |
url |
http://hdl.handle.net/10261/149838 https://doi.org/10.1016/j.foodchem.2015.04.095 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
Sí doi:10.1016/j.foodchem.2015.04.095 issn: 0308-8146 Food Chemistry 187: 225-229 (2015) http://hdl.handle.net/10261/149838 |
op_rights |
none |
op_doi |
https://doi.org/10.1016/j.foodchem.2015.04.095 |
container_title |
Food Chemistry |
container_volume |
187 |
container_start_page |
225 |
op_container_end_page |
229 |
_version_ |
1790608881979752448 |