Portal de Periódicos da CAPES

Enzymatic synthesis of optically active ferrocenes by immobilized lipase fromCandida Antarctica

1999; Wiley; Volume: 74; Issue: 6 Linguagem: Inglês

10.1002/(sici)1097-4660(199906)74

1097-4660

Toshiki Kijima, Yoshihiro Yaginuma, Taeko Izumi,

Carbohydrate Chemistry and Synthesis

Journal of Chemical Technology & BiotechnologyVolume 74, Issue 6 p. 501-508 Paper Enzymatic synthesis of optically active ferrocenes by immobilized lipase from Candida Antarctica Tatsuro Kijima, Corresponding Author Tatsuro Kijima Department of Materials Science and Technology, Faculty of Engineering, Yamagata University, Yonezawa 992, Japan.Department of Materials Science and Technology, Faculty of Engineering, Yamagata University, Yonezawa 992, Japan===Search for more papers by this authorYoshihiro Yaginuma, Yoshihiro Yaginuma Department of Materials Science and Technology, Faculty of Engineering, Yamagata University, Yonezawa 992, Japan.Search for more papers by this authorTaeko Izumi, Taeko Izumi Department of Materials Science and Technology, Faculty of Engineering, Yamagata University, Yonezawa 992, Japan.Search for more papers by this author Tatsuro Kijima, Corresponding Author Tatsuro Kijima Department of Materials Science and Technology, Faculty of Engineering, Yamagata University, Yonezawa 992, Japan.Department of Materials Science and Technology, Faculty of Engineering, Yamagata University, Yonezawa 992, Japan===Search for more papers by this authorYoshihiro Yaginuma, Yoshihiro Yaginuma Department of Materials Science and Technology, Faculty of Engineering, Yamagata University, Yonezawa 992, Japan.Search for more papers by this authorTaeko Izumi, Taeko Izumi Department of Materials Science and Technology, Faculty of Engineering, Yamagata University, Yonezawa 992, Japan.Search for more papers by this author First published: 02 June 1999 https://doi.org/10.1002/(SICI)1097-4660(199906)74:6 3.0.CO;2-6Citations: 14AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract Immobilized lipase (Candida Antarctica lipase, CAL) efficiently catalyzes the transesterification and amidation of the racemic ferrocenes, 1-hydroxyethylferrocene, (±)-1, 1-hydroxy[3](1,1′) ferrocenophane, (±)-4, 1-amonoethylferrocene, (±)-2, and 1-amono[3](1,1′) ferrocenophane, (±)-5, with acyl esters, resulting in the formation of R products possessing high enantiomeric purity. When 1-hydroxyethylferrocene, (±)-1, and 1-hydroxy[3](1,1′) ferrocenophane, (±)-4, was used as substrate diisopropyl ether was a suitable solvent. In the reaction conditions investigated, the use of vinyl acetate in diisopropyl ether gave the best yield of (R)-1a (49%, 99% ee) after 2 h of incubation at 30 °C. But, with the amino ferrocenes, 1-amonoethylferrocene, (±)-2, and 1-amono[3](1,1′) ferrocenophane, (±)-5, as substrate, diisopropyl ether was unsuitable as a solvent owing to the low solubility of the substrate in this solvent. Using tetrahydrofuran as a solvent, enzymatic amidation of 1-amonoethylferrocene, (±)-2, gave the best yield of (R)-2a (21%, 99% ee) after 120 h of incubation at 30 °C. CAL working in organic solvent is able to efficiently carry out the resolution of ferrocenyl alcohol and amine derivatives which have similar structures, such as (±)-1 and (±)-2, (±)-4 and (±)-5 which possess central chirality. This enzyme accepted only non-bulky primary alcohols and amines as ferrocenyl substrates. © 1999 Society of Chemical Industry Citing Literature Volume74, Issue6June 1999Pages 501-508 RelatedInformation