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...
Published in: | Scientific Reports |
---|---|
Main Authors: | , , , , , |
Format: | Text |
Language: | English |
Published: |
Nature Publishing Group
2017
|
Subjects: | |
Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5357956/ http://www.ncbi.nlm.nih.gov/pubmed/28317884 https://doi.org/10.1038/srep44599 |
id |
ftpubmed:oai:pubmedcentral.nih.gov:5357956 |
---|---|
record_format |
openpolar |
spelling |
ftpubmed:oai:pubmedcentral.nih.gov:5357956 2023-05-15T13:39:48+02:00 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 2017-03-20 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5357956/ http://www.ncbi.nlm.nih.gov/pubmed/28317884 https://doi.org/10.1038/srep44599 en eng Nature Publishing Group http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5357956/ http://www.ncbi.nlm.nih.gov/pubmed/28317884 http://dx.doi.org/10.1038/srep44599 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/ CC-BY Article Text 2017 ftpubmed https://doi.org/10.1038/srep44599 2017-03-26T01:13:52Z 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. Text Antarc* Antarctica PubMed Central (PMC) Scientific Reports 7 1 |
institution |
Open Polar |
collection |
PubMed Central (PMC) |
op_collection_id |
ftpubmed |
language |
English |
topic |
Article |
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 |
topic_facet |
Article |
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. |
format |
Text |
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 |
title |
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_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_sort |
engineering a lipase b from candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity |
publisher |
Nature Publishing Group |
publishDate |
2017 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5357956/ http://www.ncbi.nlm.nih.gov/pubmed/28317884 https://doi.org/10.1038/srep44599 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5357956/ http://www.ncbi.nlm.nih.gov/pubmed/28317884 http://dx.doi.org/10.1038/srep44599 |
op_rights |
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/ |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1038/srep44599 |
container_title |
Scientific Reports |
container_volume |
7 |
container_issue |
1 |
_version_ |
1766125110212689920 |