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Selective enzymatic esterification of lignin model compounds in the ball mill

A lipase-catalyzed esterification of lignin model compounds in the ball mill was developed combining the advantages of enzyme catalysis and mechanochemistry. Under the described conditions, the primary aliphatic hydroxy groups present in the substrates were selectively modified by the biocatalyst to...

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Autores principales: Weißbach, Ulla, Dabral, Saumya, Konnert, Laure, Bolm, Carsten, Hernández, José G
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Beilstein-Institut 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5588541/
https://www.ncbi.nlm.nih.gov/pubmed/28904622
http://dx.doi.org/10.3762/bjoc.13.173
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author Weißbach, Ulla
Dabral, Saumya
Konnert, Laure
Bolm, Carsten
Hernández, José G
author_facet Weißbach, Ulla
Dabral, Saumya
Konnert, Laure
Bolm, Carsten
Hernández, José G
author_sort Weißbach, Ulla
collection PubMed
description A lipase-catalyzed esterification of lignin model compounds in the ball mill was developed combining the advantages of enzyme catalysis and mechanochemistry. Under the described conditions, the primary aliphatic hydroxy groups present in the substrates were selectively modified by the biocatalyst to afford monoesterified products. Amongst the tested lipases, CALB proved to be the most effective biocatalyst for these transformations. Noteworthy, various acyl donors of different chain lengths were tolerated under the mechanochemical conditions.
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spelling pubmed-55885412017-09-13 Selective enzymatic esterification of lignin model compounds in the ball mill Weißbach, Ulla Dabral, Saumya Konnert, Laure Bolm, Carsten Hernández, José G Beilstein J Org Chem Full Research Paper A lipase-catalyzed esterification of lignin model compounds in the ball mill was developed combining the advantages of enzyme catalysis and mechanochemistry. Under the described conditions, the primary aliphatic hydroxy groups present in the substrates were selectively modified by the biocatalyst to afford monoesterified products. Amongst the tested lipases, CALB proved to be the most effective biocatalyst for these transformations. Noteworthy, various acyl donors of different chain lengths were tolerated under the mechanochemical conditions. Beilstein-Institut 2017-08-25 /pmc/articles/PMC5588541/ /pubmed/28904622 http://dx.doi.org/10.3762/bjoc.13.173 Text en Copyright © 2017, Weißbach et al. https://creativecommons.org/licenses/by/4.0https://www.beilstein-journals.org/bjoc/termsThis is an Open Access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The license is subject to the Beilstein Journal of Organic Chemistry terms and conditions: (https://www.beilstein-journals.org/bjoc/terms)
spellingShingle Full Research Paper
Weißbach, Ulla
Dabral, Saumya
Konnert, Laure
Bolm, Carsten
Hernández, José G
Selective enzymatic esterification of lignin model compounds in the ball mill
title Selective enzymatic esterification of lignin model compounds in the ball mill
title_full Selective enzymatic esterification of lignin model compounds in the ball mill
title_fullStr Selective enzymatic esterification of lignin model compounds in the ball mill
title_full_unstemmed Selective enzymatic esterification of lignin model compounds in the ball mill
title_short Selective enzymatic esterification of lignin model compounds in the ball mill
title_sort selective enzymatic esterification of lignin model compounds in the ball mill
topic Full Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5588541/
https://www.ncbi.nlm.nih.gov/pubmed/28904622
http://dx.doi.org/10.3762/bjoc.13.173
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