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Light‐Driven Enzymatic Decarboxylation of Dicarboxylic Acids
Photodecarboxylase from Chlorella variabillis (CvFAP) is one of the three known light‐activated enzymes that catalyzes the decarboxylation of fatty acids into the corresponding C1‐shortened alkanes. Although the substrate scope of CvFAP has been altered by protein engineering and decoy molecules, it...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8095292/ https://www.ncbi.nlm.nih.gov/pubmed/33945237 http://dx.doi.org/10.1002/open.202100039 |
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author | Zeng, Yong‐Yi Liu, Lan Chen, Bi‐Shuang Zhang, Wuyuan |
author_facet | Zeng, Yong‐Yi Liu, Lan Chen, Bi‐Shuang Zhang, Wuyuan |
author_sort | Zeng, Yong‐Yi |
collection | PubMed |
description | Photodecarboxylase from Chlorella variabillis (CvFAP) is one of the three known light‐activated enzymes that catalyzes the decarboxylation of fatty acids into the corresponding C1‐shortened alkanes. Although the substrate scope of CvFAP has been altered by protein engineering and decoy molecules, it is still limited to mono‐fatty acids. Our studies demonstrate for the first time that long chain dicarboxylic acids can be converted by CvFAP. Notably, the conversion of dicarboxylic acids to alkanes still represents a chemically very challenging reaction. Herein, the light‐driven enzymatic decarboxylation of dicarboxylic acids to the corresponding (C2‐shortened) alkanes using CvFAP is described. A series of dicarboxylic acids is decarboxylated into alkanes in good yields by means of this approach, even for the preparative scales. Reaction pathway studies show that mono‐fatty acids are formed as the intermediate products before the final release of C2‐shortened alkanes. In addition, the thermostability, storage stability, and recyclability of CvFAP for decarboxylation of dicarboxylic acids are well evaluated. These results represent an advancement over the current state‐of‐the‐art. |
format | Online Article Text |
id | pubmed-8095292 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-80952922021-05-10 Light‐Driven Enzymatic Decarboxylation of Dicarboxylic Acids Zeng, Yong‐Yi Liu, Lan Chen, Bi‐Shuang Zhang, Wuyuan ChemistryOpen Full Papers Photodecarboxylase from Chlorella variabillis (CvFAP) is one of the three known light‐activated enzymes that catalyzes the decarboxylation of fatty acids into the corresponding C1‐shortened alkanes. Although the substrate scope of CvFAP has been altered by protein engineering and decoy molecules, it is still limited to mono‐fatty acids. Our studies demonstrate for the first time that long chain dicarboxylic acids can be converted by CvFAP. Notably, the conversion of dicarboxylic acids to alkanes still represents a chemically very challenging reaction. Herein, the light‐driven enzymatic decarboxylation of dicarboxylic acids to the corresponding (C2‐shortened) alkanes using CvFAP is described. A series of dicarboxylic acids is decarboxylated into alkanes in good yields by means of this approach, even for the preparative scales. Reaction pathway studies show that mono‐fatty acids are formed as the intermediate products before the final release of C2‐shortened alkanes. In addition, the thermostability, storage stability, and recyclability of CvFAP for decarboxylation of dicarboxylic acids are well evaluated. These results represent an advancement over the current state‐of‐the‐art. John Wiley and Sons Inc. 2021-05-04 /pmc/articles/PMC8095292/ /pubmed/33945237 http://dx.doi.org/10.1002/open.202100039 Text en © 2021 The Authors. Published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Full Papers Zeng, Yong‐Yi Liu, Lan Chen, Bi‐Shuang Zhang, Wuyuan Light‐Driven Enzymatic Decarboxylation of Dicarboxylic Acids |
title | Light‐Driven Enzymatic Decarboxylation of Dicarboxylic Acids |
title_full | Light‐Driven Enzymatic Decarboxylation of Dicarboxylic Acids |
title_fullStr | Light‐Driven Enzymatic Decarboxylation of Dicarboxylic Acids |
title_full_unstemmed | Light‐Driven Enzymatic Decarboxylation of Dicarboxylic Acids |
title_short | Light‐Driven Enzymatic Decarboxylation of Dicarboxylic Acids |
title_sort | light‐driven enzymatic decarboxylation of dicarboxylic acids |
topic | Full Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8095292/ https://www.ncbi.nlm.nih.gov/pubmed/33945237 http://dx.doi.org/10.1002/open.202100039 |
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