KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM Candida antarctica B
The development of methodologies for obtaining chiral compounds constitutes a major challenge on current chemistry. In this context, kinetic resolution catalyzed by lipases represents an excellent alternative. In homogeneous media, these enzymes display an equilibrium between two conformations (open...
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School of Pharmaceutical and Food Sciences, University of Antioquia
2011
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ftuniantioqojs:oai:ojs.pkp.sfu.ca:article/8775 2023-05-15T13:40:15+02:00 KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM Candida antarctica B RESOLUCIÓN CINÉTICA DE (R,S)-MANDELATO DE METILO POR PREPARACIONES INMOVILIZADAS DE LIPASA DE Candida antarctica B 2011-05-17 application/pdf https://revistas.udea.edu.co/index.php/vitae/article/view/8775 eng eng School of Pharmaceutical and Food Sciences, University of Antioquia https://revistas.udea.edu.co/index.php/vitae/article/view/8775/8079 https://revistas.udea.edu.co/index.php/vitae/article/view/8775 Vitae; Vol. 18 No. 1 (2011); 33-41 Vitae; Vol. 18 Núm. 1 (2011); 33-41 2145-2660 0121-4004 Lipasas biotransformación ingeniería de proteínas enzimas inmovilizadas Lipases biotransformation protein engineering immobilized enzymes info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 2011 ftuniantioqojs 2023-01-13T07:13:09Z The development of methodologies for obtaining chiral compounds constitutes a major challenge on current chemistry. In this context, kinetic resolution catalyzed by lipases represents an excellent alternative. In homogeneous media, these enzymes display an equilibrium between two conformations (open and closed form), that can be displaced towards an open conformation (active form) in presence of hydrophobic supports. In this article lipase from Candida antarctica B (CAL-B) was purified and covalently immobilized onto Eupergit C epoxy supports (EC), Eupergit C activated with other functional groups and octyl-agarose supports. These preparations of immobilized enzymes were used under different pH conditions in the kinetic resolution of (R,S)-methyl mandelate. In this study, EC-amino-CAL-B immobilized derivative was highlighted because it is highly enantioselective at pH 8 (enantiomeric ratio (E) of 52), allowing to obtain an R-enantiomer from mandelic acid with an enantiomeric excess (ee) of 96%. El desarrollo de métodos para la obtención de compuestos quirales constituye uno de los grandes desafíos de la química actual. En este contexto, la resolución cinética catalizada por lipasas representa una excelente alternativa. En medios homogéneos, estas enzimas presentan equilibrio entre dos conformaciones (abierta y cerrada), el cual es posible desplazar hacia la conformación abierta (forma activa) en presencia de soportes hidrofóbicos. En este trabajo, la lipasa de Candida antarctica B (CAL-B) se purificó e inmovilizó covalentemente en soportes epóxido Eupergit C (EC), Eupergit C activados con otros grupos funcionales y soportes de octil-agarosa. Estas preparaciones de enzima inmovilizada se utilizaron bajo diferentes condiciones de pH en la resolución cinética del (R,S)-mandelato de metilo. Se destacó el derivado inmovilizado EC-amino-CAL-B, por ser altamente enantioselectivo a pH 8 (razón enantiomérica (E) de 52), permitiendo obtener el enantiómero R del ácido mandélico con un exceso enantiomérico (ee) del 96%. Article in Journal/Newspaper Antarc* Antarctica Universidad de Antioquia: E-Journals UdeA |
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Open Polar |
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Universidad de Antioquia: E-Journals UdeA |
op_collection_id |
ftuniantioqojs |
language |
English |
topic |
Lipasas biotransformación ingeniería de proteínas enzimas inmovilizadas Lipases biotransformation protein engineering immobilized enzymes |
spellingShingle |
Lipasas biotransformación ingeniería de proteínas enzimas inmovilizadas Lipases biotransformation protein engineering immobilized enzymes KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM Candida antarctica B |
topic_facet |
Lipasas biotransformación ingeniería de proteínas enzimas inmovilizadas Lipases biotransformation protein engineering immobilized enzymes |
description |
The development of methodologies for obtaining chiral compounds constitutes a major challenge on current chemistry. In this context, kinetic resolution catalyzed by lipases represents an excellent alternative. In homogeneous media, these enzymes display an equilibrium between two conformations (open and closed form), that can be displaced towards an open conformation (active form) in presence of hydrophobic supports. In this article lipase from Candida antarctica B (CAL-B) was purified and covalently immobilized onto Eupergit C epoxy supports (EC), Eupergit C activated with other functional groups and octyl-agarose supports. These preparations of immobilized enzymes were used under different pH conditions in the kinetic resolution of (R,S)-methyl mandelate. In this study, EC-amino-CAL-B immobilized derivative was highlighted because it is highly enantioselective at pH 8 (enantiomeric ratio (E) of 52), allowing to obtain an R-enantiomer from mandelic acid with an enantiomeric excess (ee) of 96%. El desarrollo de métodos para la obtención de compuestos quirales constituye uno de los grandes desafíos de la química actual. En este contexto, la resolución cinética catalizada por lipasas representa una excelente alternativa. En medios homogéneos, estas enzimas presentan equilibrio entre dos conformaciones (abierta y cerrada), el cual es posible desplazar hacia la conformación abierta (forma activa) en presencia de soportes hidrofóbicos. En este trabajo, la lipasa de Candida antarctica B (CAL-B) se purificó e inmovilizó covalentemente en soportes epóxido Eupergit C (EC), Eupergit C activados con otros grupos funcionales y soportes de octil-agarosa. Estas preparaciones de enzima inmovilizada se utilizaron bajo diferentes condiciones de pH en la resolución cinética del (R,S)-mandelato de metilo. Se destacó el derivado inmovilizado EC-amino-CAL-B, por ser altamente enantioselectivo a pH 8 (razón enantiomérica (E) de 52), permitiendo obtener el enantiómero R del ácido mandélico con un exceso enantiomérico (ee) del 96%. |
format |
Article in Journal/Newspaper |
title |
KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM Candida antarctica B |
title_short |
KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM Candida antarctica B |
title_full |
KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM Candida antarctica B |
title_fullStr |
KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM Candida antarctica B |
title_full_unstemmed |
KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM Candida antarctica B |
title_sort |
kinetic resolution of (r,s)-methyl mandelate by immobilized lipase preparations from candida antarctica b |
publisher |
School of Pharmaceutical and Food Sciences, University of Antioquia |
publishDate |
2011 |
url |
https://revistas.udea.edu.co/index.php/vitae/article/view/8775 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Vitae; Vol. 18 No. 1 (2011); 33-41 Vitae; Vol. 18 Núm. 1 (2011); 33-41 2145-2660 0121-4004 |
op_relation |
https://revistas.udea.edu.co/index.php/vitae/article/view/8775/8079 https://revistas.udea.edu.co/index.php/vitae/article/view/8775 |
_version_ |
1766131507292798976 |