Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity

A Ser105Ala mutant of the lipase B from Candida antarctica enables ‘perhydrolase-only’ reactions. At the example of the chemoenzymatic Baeyer-Villiger oxidation of cyclohexanone, we demonstrate that with this mutant selective oxidation can be achieved in deep eutectic solvent while essentially elimi...

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Autores principales: Wang, Xu-Ping, Zhou, Peng-Fei, Li, Zhi-Gang, Yang, Bo, Hollmann, Frank, Wang, Yong-Hua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5357956/
https://www.ncbi.nlm.nih.gov/pubmed/28317884
http://dx.doi.org/10.1038/srep44599
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author Wang, Xu-Ping
Zhou, Peng-Fei
Li, Zhi-Gang
Yang, Bo
Hollmann, Frank
Wang, Yong-Hua
author_facet Wang, Xu-Ping
Zhou, Peng-Fei
Li, Zhi-Gang
Yang, Bo
Hollmann, Frank
Wang, Yong-Hua
author_sort Wang, Xu-Ping
collection PubMed
description A Ser105Ala mutant of the lipase B from Candida antarctica enables ‘perhydrolase-only’ reactions. At the example of the chemoenzymatic Baeyer-Villiger oxidation of cyclohexanone, we demonstrate that with this mutant selective oxidation can be achieved in deep eutectic solvent while essentially eliminating the undesired hydrolysis reaction of the product.
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spelling pubmed-53579562017-03-22 Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity Wang, Xu-Ping Zhou, Peng-Fei Li, Zhi-Gang Yang, Bo Hollmann, Frank Wang, Yong-Hua Sci Rep Article A Ser105Ala mutant of the lipase B from Candida antarctica enables ‘perhydrolase-only’ reactions. At the example of the chemoenzymatic Baeyer-Villiger oxidation of cyclohexanone, we demonstrate that with this mutant selective oxidation can be achieved in deep eutectic solvent while essentially eliminating the undesired hydrolysis reaction of the product. Nature Publishing Group 2017-03-20 /pmc/articles/PMC5357956/ /pubmed/28317884 http://dx.doi.org/10.1038/srep44599 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Wang, Xu-Ping
Zhou, Peng-Fei
Li, Zhi-Gang
Yang, Bo
Hollmann, Frank
Wang, Yong-Hua
Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity
title Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity
title_full Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity
title_fullStr Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity
title_full_unstemmed Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity
title_short Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity
title_sort engineering a lipase b from candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5357956/
https://www.ncbi.nlm.nih.gov/pubmed/28317884
http://dx.doi.org/10.1038/srep44599
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