Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols
Chiral tertiary alcohols are important organic compounds in science as well as in industry. However, their preparation in enantiomerically pure form is still a challenge due to their complex structure and steric hindrances compared with primary and secondary alcohols, so kinetic resolution could be...
Published in: | ChemBioChem |
---|---|
Main Authors: | , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2024
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1002/cbic.202400082 |
id |
crwiley:10.1002/cbic.202400082 |
---|---|
record_format |
openpolar |
spelling |
crwiley:10.1002/cbic.202400082 2024-06-23T07:47:45+00:00 Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols Wagner, Karla Hummel, Anke Yang, Jianing Horino, Satoshi Kanomata, Kyohei Akai, Shuji Gröger, Harald 2024 http://dx.doi.org/10.1002/cbic.202400082 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor ChemBioChem ISSN 1439-4227 1439-7633 journal-article 2024 crwiley https://doi.org/10.1002/cbic.202400082 2024-06-11T04:43:52Z Chiral tertiary alcohols are important organic compounds in science as well as in industry. However, their preparation in enantiomerically pure form is still a challenge due to their complex structure and steric hindrances compared with primary and secondary alcohols, so kinetic resolution could be an attractive approach. Lipase A from Candida antarctica (CAL‐A) has been shown to catalyze the enantioselective esterification of various tertiary alcohols with excellent enantioselectivity but low activity. Here we report a mutagenesis study by rational design to improve CAL‐A activity against tertiary alcohols. Single mutants of CAL‐A were selected, expressed, immobilized and screened for esterification of the tertiary alcohol 1,2,3,4‐tetrahydronaphthalene‐1‐ol. A double mutant V278S+S429G showed a 1.5‐fold higher reaction rate than that of the wild type CAL‐A, while maintaining excellent enantioselectivity. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library ChemBioChem |
institution |
Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
Chiral tertiary alcohols are important organic compounds in science as well as in industry. However, their preparation in enantiomerically pure form is still a challenge due to their complex structure and steric hindrances compared with primary and secondary alcohols, so kinetic resolution could be an attractive approach. Lipase A from Candida antarctica (CAL‐A) has been shown to catalyze the enantioselective esterification of various tertiary alcohols with excellent enantioselectivity but low activity. Here we report a mutagenesis study by rational design to improve CAL‐A activity against tertiary alcohols. Single mutants of CAL‐A were selected, expressed, immobilized and screened for esterification of the tertiary alcohol 1,2,3,4‐tetrahydronaphthalene‐1‐ol. A double mutant V278S+S429G showed a 1.5‐fold higher reaction rate than that of the wild type CAL‐A, while maintaining excellent enantioselectivity. |
format |
Article in Journal/Newspaper |
author |
Wagner, Karla Hummel, Anke Yang, Jianing Horino, Satoshi Kanomata, Kyohei Akai, Shuji Gröger, Harald |
spellingShingle |
Wagner, Karla Hummel, Anke Yang, Jianing Horino, Satoshi Kanomata, Kyohei Akai, Shuji Gröger, Harald Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols |
author_facet |
Wagner, Karla Hummel, Anke Yang, Jianing Horino, Satoshi Kanomata, Kyohei Akai, Shuji Gröger, Harald |
author_sort |
Wagner, Karla |
title |
Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols |
title_short |
Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols |
title_full |
Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols |
title_fullStr |
Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols |
title_full_unstemmed |
Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols |
title_sort |
protein engineering of lipase a from candida antarctica to improve esterification of tertiary alcohols |
publisher |
Wiley |
publishDate |
2024 |
url |
http://dx.doi.org/10.1002/cbic.202400082 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ChemBioChem ISSN 1439-4227 1439-7633 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/cbic.202400082 |
container_title |
ChemBioChem |
_version_ |
1802637900856164352 |