Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid

The fatty acid photodecarboxylase from Chlorella variabilis NC64 A (CvFAP) catalyses the light‐dependent decarboxylation of fatty acids. Photoinactivation of CvFAP still represents one of the major limitations of this interesting enzyme en route to practical application. In this study we demonstrate...

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Autores principales: Wu, Yinqi, Paul, Caroline E., Hollmann, Frank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8362199/
https://www.ncbi.nlm.nih.gov/pubmed/34002919
http://dx.doi.org/10.1002/cbic.202100182
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author Wu, Yinqi
Paul, Caroline E.
Hollmann, Frank
author_facet Wu, Yinqi
Paul, Caroline E.
Hollmann, Frank
author_sort Wu, Yinqi
collection PubMed
description The fatty acid photodecarboxylase from Chlorella variabilis NC64 A (CvFAP) catalyses the light‐dependent decarboxylation of fatty acids. Photoinactivation of CvFAP still represents one of the major limitations of this interesting enzyme en route to practical application. In this study we demonstrate that the photostability of CvFAP can easily be improved by the administration of medium‐chain length carboxylic acids such as caprylic acid indicating that the best way of maintaining CvFAP stability is ‘to keep the enzyme busy’.
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spelling pubmed-83621992021-08-17 Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid Wu, Yinqi Paul, Caroline E. Hollmann, Frank Chembiochem Communications The fatty acid photodecarboxylase from Chlorella variabilis NC64 A (CvFAP) catalyses the light‐dependent decarboxylation of fatty acids. Photoinactivation of CvFAP still represents one of the major limitations of this interesting enzyme en route to practical application. In this study we demonstrate that the photostability of CvFAP can easily be improved by the administration of medium‐chain length carboxylic acids such as caprylic acid indicating that the best way of maintaining CvFAP stability is ‘to keep the enzyme busy’. John Wiley and Sons Inc. 2021-06-01 2021-07-15 /pmc/articles/PMC8362199/ /pubmed/34002919 http://dx.doi.org/10.1002/cbic.202100182 Text en © 2021 The Authors. ChemBioChem published by Wiley-VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
Wu, Yinqi
Paul, Caroline E.
Hollmann, Frank
Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid
title Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid
title_full Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid
title_fullStr Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid
title_full_unstemmed Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid
title_short Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid
title_sort stabilisation of the fatty acid decarboxylase from chlorella variabilis by caprylic acid
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8362199/
https://www.ncbi.nlm.nih.gov/pubmed/34002919
http://dx.doi.org/10.1002/cbic.202100182
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AT paulcarolinee stabilisationofthefattyaciddecarboxylasefromchlorellavariabilisbycaprylicacid
AT hollmannfrank stabilisationofthefattyaciddecarboxylasefromchlorellavariabilisbycaprylicacid

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