Kinetic resolution of 1,1′-binaphthylamines via lipase-catalyzed amidation
✍ Scribed by Naoto Aoyagi; Taeko Izumi
- Book ID
- 104251555
- Publisher
- Elsevier Science
- Year
- 2002
- Tongue
- French
- Weight
- 127 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0040-4039
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✦ Synopsis
Lipase-catalyzed amidation of 2-(2-aminoethyl)-1,1%-binaphthyl (±)-3 gave optically active 2-[2-(acylamino)ethyl]-1,1%binaphthyls (R)-6a-c with high enantiomeric excess.
📜 SIMILAR VOLUMES
Acenaphthenyl acetate and acenaphthenol are resolved through Pseudomonas fluorescens lipase (PFL)-catalyzed hydrolysis and acylation, respectively. By contrast, the structurally related 1-(1-naphthyl)ethyl acetate and 1-(1naphthyl)ethanol are inactive under the same reaction conditions.
The enzymatic dynamic kinetic resolution of N-acylhemiaminals by various lipases, namely, lipase PS, lipase AK and lipase QL, has been investigated. The acetylation of racemic N-acylhemiaminals with lipases exclusively produced the (R)-enantiomers in enantiomerically pure form and quantitative yield