Protein Engineering of Lipase A from Candida Antarctica to Improve Esterification of Tertiary Alcohols
Abstract: 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‐tetrahydronaphthalen‐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.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Protein Engineering of Lipase A from Candida Antarctica to Improve Esterification of Tertiary Alcohols ; volume:25 ; number:24 ; year:2024 ; extent:8
ChemBioChem ; 25, Heft 24 (2024) (gesamt 8)
- Creator
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Wagner, Karla
Hummel, Anke
Yang, Jianing
Horino, Satoshi
Kanomata, Kyohei
Akai, Shuji
Gröger, Harald
- DOI
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10.1002/cbic.202400082
- URN
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urn:nbn:de:101:1-2412241305547.261199749777
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:28 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Wagner, Karla
- Hummel, Anke
- Yang, Jianing
- Horino, Satoshi
- Kanomata, Kyohei
- Akai, Shuji
- Gröger, Harald