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Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine

Lipases from Geotrichum candidum 4013 (extracellular lipase and cell-bound lipase) were immobilized by adsorption on chitosan beads. The enzyme preparations were tested in the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine in dimethylformamide with different vinyl esters (ac...

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Detalles Bibliográficos
Autores principales: Brabcová, Jana, Blažek, Jiří, Janská, Lucie, Krečmerová, Marcela, Zarevúcka, Marie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6268494/
https://www.ncbi.nlm.nih.gov/pubmed/23174898
http://dx.doi.org/10.3390/molecules171213813
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author Brabcová, Jana
Blažek, Jiří
Janská, Lucie
Krečmerová, Marcela
Zarevúcka, Marie
author_facet Brabcová, Jana
Blažek, Jiří
Janská, Lucie
Krečmerová, Marcela
Zarevúcka, Marie
author_sort Brabcová, Jana
collection PubMed
description Lipases from Geotrichum candidum 4013 (extracellular lipase and cell-bound lipase) were immobilized by adsorption on chitosan beads. The enzyme preparations were tested in the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine in dimethylformamide with different vinyl esters (acetate, butyrate, decanoate, laurate, palmitate). The transesterification activities of these immobilized enzymes were compared with commercially available lipases (lipase from hog pancreas, Aspergillus niger, Candida antarctica, Pseudomonas fluorescens). Lipase from Candida antarctica was found to be the most efficient enzyme regarding chemical yield of the desired products, while transesterification by lipase from Aspergillus niger resulted in lower yields.
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spelling pubmed-62684942018-12-14 Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine Brabcová, Jana Blažek, Jiří Janská, Lucie Krečmerová, Marcela Zarevúcka, Marie Molecules Article Lipases from Geotrichum candidum 4013 (extracellular lipase and cell-bound lipase) were immobilized by adsorption on chitosan beads. The enzyme preparations were tested in the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine in dimethylformamide with different vinyl esters (acetate, butyrate, decanoate, laurate, palmitate). The transesterification activities of these immobilized enzymes were compared with commercially available lipases (lipase from hog pancreas, Aspergillus niger, Candida antarctica, Pseudomonas fluorescens). Lipase from Candida antarctica was found to be the most efficient enzyme regarding chemical yield of the desired products, while transesterification by lipase from Aspergillus niger resulted in lower yields. MDPI 2012-11-22 /pmc/articles/PMC6268494/ /pubmed/23174898 http://dx.doi.org/10.3390/molecules171213813 Text en © 2012 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 Article
Brabcová, Jana
Blažek, Jiří
Janská, Lucie
Krečmerová, Marcela
Zarevúcka, Marie
Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine
title Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine
title_full Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine
title_fullStr Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine
title_full_unstemmed Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine
title_short Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine
title_sort lipases as tools in the synthesis of prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6268494/
https://www.ncbi.nlm.nih.gov/pubmed/23174898
http://dx.doi.org/10.3390/molecules171213813
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