KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> 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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Autores principales:	Jenifer CRUZ, Rodrigo TORRES, Claudia ORTIZ
Formato:	article
Lenguaje:	EN
Publicado:	Universidad de Antioquia 2011
Materias:	Lipases biotransformation protein engineering immobilized enzymes. Food processing and manufacture TP368-456 Pharmaceutical industry HD9665-9675
Acceso en línea:	https://doaj.org/article/b8a5572b8874465abee176833b973d1c
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spelling	oai:doaj.org-article:b8a5572b8874465abee176833b973d1c2021-11-19T04:14:08ZKINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> B0121-40042145-2660https://doaj.org/article/b8a5572b8874465abee176833b973d1c2011-05-01T00:00:00Zhttps://revistas.udea.edu.co/index.php/vitae/article/view/8775https://doaj.org/toc/0121-4004https://doaj.org/toc/2145-2660The 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%.Jenifer CRUZRodrigo TORRESClaudia ORTIZUniversidad de AntioquiaarticleLipasesbiotransformationprotein engineeringimmobilized enzymes.Food processing and manufactureTP368-456Pharmaceutical industryHD9665-9675ENVitae, Vol 18, Iss 1 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Lipases biotransformation protein engineering immobilized enzymes. Food processing and manufacture TP368-456 Pharmaceutical industry HD9665-9675
spellingShingle	Lipases biotransformation protein engineering immobilized enzymes. Food processing and manufacture TP368-456 Pharmaceutical industry HD9665-9675 Jenifer CRUZ Rodrigo TORRES Claudia ORTIZ KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> B
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%.
format	article
author	Jenifer CRUZ Rodrigo TORRES Claudia ORTIZ
author_facet	Jenifer CRUZ Rodrigo TORRES Claudia ORTIZ
author_sort	Jenifer CRUZ
title	KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> B
title_short	KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> B
title_full	KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> B
title_fullStr	KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> B
title_full_unstemmed	KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> B
title_sort	kinetic resolution of (r,s)-methyl mandelate by immobilized lipase preparations from <i>candida antarctica</i> b
publisher	Universidad de Antioquia
publishDate	2011
url	https://doaj.org/article/b8a5572b8874465abee176833b973d1c
work_keys_str_mv	AT jenifercruz kineticresolutionofrsmethylmandelatebyimmobilizedlipasepreparationsfromicandidaantarcticaib AT rodrigotorres kineticresolutionofrsmethylmandelatebyimmobilizedlipasepreparationsfromicandidaantarcticaib AT claudiaortiz kineticresolutionofrsmethylmandelatebyimmobilizedlipasepreparationsfromicandidaantarcticaib
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KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> B

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