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Chemoenzymatic Kinetic resolution of (R)-malathion in aqueous media
BACKGROUND: Malathion (R,S)-diethyl-2-[(dimethoxyphosphorothioyl)sulfanyl]butanedioate is a chiral organophosphorus compound used widely as pesticide for suppression of harmful insects such as mosquitoes. It is well known that in biological systems (R)-malathion is the active enantiomer, therefore a...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4564436/ https://www.ncbi.nlm.nih.gov/pubmed/26361495 http://dx.doi.org/10.1186/s13065-015-0119-y |
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author | Enríquez-Núñez, Carlos A. Camacho-Dávila, Alejandro A. Ramos-Sánchez, Víctor H. Zaragoza-Galán, Gerardo Ballinas-Casarrubias, Lourdes Chávez-Flores, David |
author_facet | Enríquez-Núñez, Carlos A. Camacho-Dávila, Alejandro A. Ramos-Sánchez, Víctor H. Zaragoza-Galán, Gerardo Ballinas-Casarrubias, Lourdes Chávez-Flores, David |
author_sort | Enríquez-Núñez, Carlos A. |
collection | PubMed |
description | BACKGROUND: Malathion (R,S)-diethyl-2-[(dimethoxyphosphorothioyl)sulfanyl]butanedioate is a chiral organophosphorus compound used widely as pesticide for suppression of harmful insects such as mosquitoes. It is well known that in biological systems (R)-malathion is the active enantiomer, therefore a sustainable approach could be the use of only the biologically active enantiomer. The resolution of the commercial racemic mixture to obtain the pure active enantiomer combined with a recycling of the undesired enantiomer through a racemization process could be an attractive alternative to reduce the environmental impact of this pesticide. Thus, this work evaluates the use of four commercially available lipases for enantioselective hydrolysis and separation of malathion enantiomers from the commercial racemic mixture. RESULTS: Several lipases were methodologically assessed, considering parameters such as enzyme concentration, temperature and reaction rates. Among them, Candida rugosa lipase exhibited the best performance, in terms of enantioselectivity, E = 185 (selective to the (S)-enantiomer). In this way, the desired unreacted (R)-enantiomer was recovered in a 49.42 % yield with an enantiomeric excess of 87 %. The monohydrolized (S)-enantiomer was recovered and racemized in basic media, followed by esterification to obtain the racemic malathion, which was recycled. In this way, an enantioenriched mixture of (R)-malathion was obtained with a conversion of 65.80 % considering the recycled (S)-enantiomer. CONCLUSION: This work demonstrated the feasibility of exploiting Candida rugosa lipase to kinetically resolve racemic malathion through an environmentally friendly recycling of the undesired (S)-enantiomer. [Figure: see text] |
format | Online Article Text |
id | pubmed-4564436 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-45644362015-09-11 Chemoenzymatic Kinetic resolution of (R)-malathion in aqueous media Enríquez-Núñez, Carlos A. Camacho-Dávila, Alejandro A. Ramos-Sánchez, Víctor H. Zaragoza-Galán, Gerardo Ballinas-Casarrubias, Lourdes Chávez-Flores, David Chem Cent J Research Article BACKGROUND: Malathion (R,S)-diethyl-2-[(dimethoxyphosphorothioyl)sulfanyl]butanedioate is a chiral organophosphorus compound used widely as pesticide for suppression of harmful insects such as mosquitoes. It is well known that in biological systems (R)-malathion is the active enantiomer, therefore a sustainable approach could be the use of only the biologically active enantiomer. The resolution of the commercial racemic mixture to obtain the pure active enantiomer combined with a recycling of the undesired enantiomer through a racemization process could be an attractive alternative to reduce the environmental impact of this pesticide. Thus, this work evaluates the use of four commercially available lipases for enantioselective hydrolysis and separation of malathion enantiomers from the commercial racemic mixture. RESULTS: Several lipases were methodologically assessed, considering parameters such as enzyme concentration, temperature and reaction rates. Among them, Candida rugosa lipase exhibited the best performance, in terms of enantioselectivity, E = 185 (selective to the (S)-enantiomer). In this way, the desired unreacted (R)-enantiomer was recovered in a 49.42 % yield with an enantiomeric excess of 87 %. The monohydrolized (S)-enantiomer was recovered and racemized in basic media, followed by esterification to obtain the racemic malathion, which was recycled. In this way, an enantioenriched mixture of (R)-malathion was obtained with a conversion of 65.80 % considering the recycled (S)-enantiomer. CONCLUSION: This work demonstrated the feasibility of exploiting Candida rugosa lipase to kinetically resolve racemic malathion through an environmentally friendly recycling of the undesired (S)-enantiomer. [Figure: see text] Springer International Publishing 2015-09-09 /pmc/articles/PMC4564436/ /pubmed/26361495 http://dx.doi.org/10.1186/s13065-015-0119-y Text en © Enríquez-Núñez et al. 2015 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Research Article Enríquez-Núñez, Carlos A. Camacho-Dávila, Alejandro A. Ramos-Sánchez, Víctor H. Zaragoza-Galán, Gerardo Ballinas-Casarrubias, Lourdes Chávez-Flores, David Chemoenzymatic Kinetic resolution of (R)-malathion in aqueous media |
title | Chemoenzymatic Kinetic resolution of (R)-malathion in aqueous media |
title_full | Chemoenzymatic Kinetic resolution of (R)-malathion in aqueous media |
title_fullStr | Chemoenzymatic Kinetic resolution of (R)-malathion in aqueous media |
title_full_unstemmed | Chemoenzymatic Kinetic resolution of (R)-malathion in aqueous media |
title_short | Chemoenzymatic Kinetic resolution of (R)-malathion in aqueous media |
title_sort | chemoenzymatic kinetic resolution of (r)-malathion in aqueous media |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4564436/ https://www.ncbi.nlm.nih.gov/pubmed/26361495 http://dx.doi.org/10.1186/s13065-015-0119-y |
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