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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Beilstein-Institut
2017
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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. |
format | Online Article Text |
id | pubmed-5588541 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Beilstein-Institut |
record_format | MEDLINE/PubMed |
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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