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Novel One-Pot Green Synthesis of Indolizines Biocatalysed by Candida antarctica Lipases

Marine microorganisms are of considerable interest as a promising source of enzymes with unsuspected potentials as catalysts for chemical synthesis. We describe here an efficient method for one-pot indolizine synthesis that has been developed using lipase A and lipase B from Candida antarctica as bi...

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Autores principales: Dinica, Rodica Mihaela, Furdui, Bianca, Ghinea, Ioana Otilia, Bahrim, Gabriela, Bonte, Simon, Demeunynck, Martine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3640390/
https://www.ncbi.nlm.nih.gov/pubmed/23389089
http://dx.doi.org/10.3390/md11020431
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author Dinica, Rodica Mihaela
Furdui, Bianca
Ghinea, Ioana Otilia
Bahrim, Gabriela
Bonte, Simon
Demeunynck, Martine
author_facet Dinica, Rodica Mihaela
Furdui, Bianca
Ghinea, Ioana Otilia
Bahrim, Gabriela
Bonte, Simon
Demeunynck, Martine
author_sort Dinica, Rodica Mihaela
collection PubMed
description Marine microorganisms are of considerable interest as a promising source of enzymes with unsuspected potentials as catalysts for chemical synthesis. We describe here an efficient method for one-pot indolizine synthesis that has been developed using lipase A and lipase B from Candida antarctica as biocatalysts. As showed by HPLC/MS analysis, the yield in indolizines was higher in the presence of the biocatalyst than in absence of enzyme. Lipase A, from Candida antarctica, showed high catalytic activity and selectivity for the cycloaddition reactions. When the reactions were performed under ultrasound irradiation, the Candida antarctica lipase catalyzed reactions yielded pure indolozines, in good yields and in very short time.
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spelling pubmed-36403902013-05-02 Novel One-Pot Green Synthesis of Indolizines Biocatalysed by Candida antarctica Lipases Dinica, Rodica Mihaela Furdui, Bianca Ghinea, Ioana Otilia Bahrim, Gabriela Bonte, Simon Demeunynck, Martine Mar Drugs Communication Marine microorganisms are of considerable interest as a promising source of enzymes with unsuspected potentials as catalysts for chemical synthesis. We describe here an efficient method for one-pot indolizine synthesis that has been developed using lipase A and lipase B from Candida antarctica as biocatalysts. As showed by HPLC/MS analysis, the yield in indolizines was higher in the presence of the biocatalyst than in absence of enzyme. Lipase A, from Candida antarctica, showed high catalytic activity and selectivity for the cycloaddition reactions. When the reactions were performed under ultrasound irradiation, the Candida antarctica lipase catalyzed reactions yielded pure indolozines, in good yields and in very short time. MDPI 2013-02-06 /pmc/articles/PMC3640390/ /pubmed/23389089 http://dx.doi.org/10.3390/md11020431 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Communication
Dinica, Rodica Mihaela
Furdui, Bianca
Ghinea, Ioana Otilia
Bahrim, Gabriela
Bonte, Simon
Demeunynck, Martine
Novel One-Pot Green Synthesis of Indolizines Biocatalysed by Candida antarctica Lipases
title Novel One-Pot Green Synthesis of Indolizines Biocatalysed by Candida antarctica Lipases
title_full Novel One-Pot Green Synthesis of Indolizines Biocatalysed by Candida antarctica Lipases
title_fullStr Novel One-Pot Green Synthesis of Indolizines Biocatalysed by Candida antarctica Lipases
title_full_unstemmed Novel One-Pot Green Synthesis of Indolizines Biocatalysed by Candida antarctica Lipases
title_short Novel One-Pot Green Synthesis of Indolizines Biocatalysed by Candida antarctica Lipases
title_sort novel one-pot green synthesis of indolizines biocatalysed by candida antarctica lipases
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3640390/
https://www.ncbi.nlm.nih.gov/pubmed/23389089
http://dx.doi.org/10.3390/md11020431
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