Lipase-catalyzed mono-O-acylation of dithiothreitol and dithioerythritol

Mono-O-acyl derivatives of dithiothreitol and dithioerythritol were obtained in 40-60% yield, through a lipase-catalyzed transesterification in organic media. Reactions were conducted in neutral conditions at moderate temperature, with or without solvent. Candida antarctica lipase resulted the most...

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Bibliographic Details
Main Authors: Iglesias, L.E., Baldessari, A., Gros, E.G.
Format: Journal/Newspaper
Language:unknown
Subjects:
Online Access:https://hdl.handle.net/20.500.12110/paper_01415492_v20_n3_p275_Iglesias
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spelling ftunibueairesbd:todo:paper_01415492_v20_n3_p275_Iglesias 2023-10-29T02:32:06+01:00 Lipase-catalyzed mono-O-acylation of dithiothreitol and dithioerythritol Iglesias, L.E. Baldessari, A. Gros, E.G. https://hdl.handle.net/20.500.12110/paper_01415492_v20_n3_p275_Iglesias unknown http://hdl.handle.net/20.500.12110/paper_01415492_v20_n3_p275_Iglesias info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar dithioerythritol dithiothreitol solvent triacylglycerol lipase acylation article candida temperature JOUR ftunibueairesbd https://doi.org/20.500.12110/paper_01415492_v20_n3_p275_Iglesias 2023-10-05T01:27:12Z Mono-O-acyl derivatives of dithiothreitol and dithioerythritol were obtained in 40-60% yield, through a lipase-catalyzed transesterification in organic media. Reactions were conducted in neutral conditions at moderate temperature, with or without solvent. Candida antarctica lipase resulted the most efficient biocatalyst (yields over 60%) when working without solvent. Fil:Iglesias, L.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Baldessari, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gros, E.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Journal/Newspaper Antarc* Antarctica Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires)
institution Open Polar
collection Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires)
op_collection_id ftunibueairesbd
language unknown
topic dithioerythritol
dithiothreitol
solvent
triacylglycerol lipase
acylation
article
candida
temperature
spellingShingle dithioerythritol
dithiothreitol
solvent
triacylglycerol lipase
acylation
article
candida
temperature
Iglesias, L.E.
Baldessari, A.
Gros, E.G.
Lipase-catalyzed mono-O-acylation of dithiothreitol and dithioerythritol
topic_facet dithioerythritol
dithiothreitol
solvent
triacylglycerol lipase
acylation
article
candida
temperature
description Mono-O-acyl derivatives of dithiothreitol and dithioerythritol were obtained in 40-60% yield, through a lipase-catalyzed transesterification in organic media. Reactions were conducted in neutral conditions at moderate temperature, with or without solvent. Candida antarctica lipase resulted the most efficient biocatalyst (yields over 60%) when working without solvent. Fil:Iglesias, L.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Baldessari, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gros, E.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
format Journal/Newspaper
author Iglesias, L.E.
Baldessari, A.
Gros, E.G.
author_facet Iglesias, L.E.
Baldessari, A.
Gros, E.G.
author_sort Iglesias, L.E.
title Lipase-catalyzed mono-O-acylation of dithiothreitol and dithioerythritol
title_short Lipase-catalyzed mono-O-acylation of dithiothreitol and dithioerythritol
title_full Lipase-catalyzed mono-O-acylation of dithiothreitol and dithioerythritol
title_fullStr Lipase-catalyzed mono-O-acylation of dithiothreitol and dithioerythritol
title_full_unstemmed Lipase-catalyzed mono-O-acylation of dithiothreitol and dithioerythritol
title_sort lipase-catalyzed mono-o-acylation of dithiothreitol and dithioerythritol
url https://hdl.handle.net/20.500.12110/paper_01415492_v20_n3_p275_Iglesias
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation http://hdl.handle.net/20.500.12110/paper_01415492_v20_n3_p275_Iglesias
op_rights info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
op_doi https://doi.org/20.500.12110/paper_01415492_v20_n3_p275_Iglesias
_version_ 1781053174064349184