Characterization of a novel amine transaminase from Halomonas elongata
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|Title:||Characterization of a novel amine transaminase from Halomonas elongata||Authors:||Cerioli, Lorenzo
|Permanent link:||http://hdl.handle.net/10197/7250||Date:||Oct-2015||Abstract:||Chiral amines are indispensable building blocks in the production of biologically active compounds. They are fundamental for the pharmaceutical industry, both as active molecules themselves and as chiral auxiliaries in asymmetric synthesis; however, the available synthetic strategies often present disadvantages. ω-Transaminases (ω-TAs) appear as an attractive alternative by driving the stereoselective amination of prochiral ketones. HEWT is a novel amine transaminase from the moderate halophilic bacterium, Halomonas elongata DSM 2581, which is highly (S)-selective, being able to fully convert (S)-1-phenylethylamine to acetophenone and showing no activity with the corresponding (R)-1-phenylethylamine. HEWT has a broad substrate scope, active with a range of amino donors and acceptors, and naturally accepts isopropylamine (IPA) as amino donor in asymmetric synthesis providing a 41% conversion of pyruvate in 24 h at 37 °C starting with 1:1 molar ratio between the reagents. HEWT also accepts ortho-xylylenediamine as amino donor in for amine synthesis, in particular, with benzaldehyde yielding high conversions between 90 and 95%. The enzyme is also tolerant to the presence of cosolvents up to 20% making it a promising candidate for industrial applications.||Funding Details:||Science Foundation Ireland||Type of material:||Journal Article||Publisher:||Elsevier||Copyright (published version):||2015 Elsevier||Keywords:||Amine transaminase;Biocatalysis;Asymmetric synthesis;Isopropylamine;o-xylylenediamine||DOI:||10.1016/j.molcatb.2015.07.009||Language:||en||Status of Item:||Peer reviewed|
|Appears in Collections:||Chemistry Research Collection|
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