Candida antarctica Lipase B in a Chemoenzymatic Route to Cyclic α‐Quaternary α‐Amino Acid Enantiomers
Abstract Kinetic resolution of three cyclic quaternary ethyl 1‐amino‐2,3‐dihydro‐1 H ‐indene‐1‐carboxylates and both 1‐ and 2‐amino‐1,2,3,4‐tetrahydronaphthalene analogues have been studied. Interesterification with butyl butanoate and Candida antarctica lipase B accomplished the task. The enantiome...
| Published in: | European Journal of Organic Chemistry |
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| Main Authors: | , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
2011
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1002/ejoc.201001575 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fejoc.201001575 http://onlinelibrary.wiley.com/wol1/doi/10.1002/ejoc.201001575/fullpdf |
| Summary: | Abstract Kinetic resolution of three cyclic quaternary ethyl 1‐amino‐2,3‐dihydro‐1 H ‐indene‐1‐carboxylates and both 1‐ and 2‐amino‐1,2,3,4‐tetrahydronaphthalene analogues have been studied. Interesterification with butyl butanoate and Candida antarctica lipase B accomplished the task. The enantiomers of all 1‐amino analogues reacted with excellent enantioselectivity (enantiomeric ratio er greater than 200), whereas the 2‐amino analogue was not enantioselective ( er = 4). Amino acid enantiomers were finally obtained as their respective hydrochlorides with almost maximum theoretical yields. For the first time, a lipase enzyme was effectively used in the kinetic resolution of cyclic α‐quaternary α‐amino esters. |
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