Immobilization of two (R)‐Amine Transaminases on an Optimized Chitosan Support for the Enzymatic Synthesis of Optically Pure Amines. Issue 2 (9th October 2012)

• Record Type: Journal Article
• Authors: Mallin, Hendrik; Menyes, Ulf; Vorhaben, Torge; Höhne, Matthias; Bornscheuer, Uwe T.
• Is Part Of: ChemCatChem. Volume 5:Issue 2(2013:Feb.)
• Page Start: 588
• Page End: 593
• Publication Date: 2012-10-09
• Subjects: Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.201200420
• Languages: English
• ISSNs: 1867-3880

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Two (<italic>R</italic>)‐selective amine transaminases from <italic>Gibberella zeae</italic> (GibZea) and from <italic>Neosartorya fischeri</italic> (NeoFis) were immobilized on chitosan as a carrier to improve their application in the biocatalytic synthesis of chiral (<italic>R</italic>)‐amines. An (<italic>S</italic>)‐selective enzyme from <italic>Vibrio fluvialis</italic> (VfTA) was used for comparison. After improving the immobilization conditions, all enzymes could be efficiently immobilized. Additionally, the thermal stability of GibZea and NeoFis could be improved and also a slight shift of the pH optimum was observed for GibZea. All enzymes showed good activity in the conversion of α‐methylbenzylamine. In the asymmetric synthesis of (<italic>R</italic>)‐2‐aminohexane from the corresponding ketone, a 13.4‐fold higher conversion (&gt;99 %) was found for the immobilized GibZea compared to the free enzyme. Hence, the covalent binding with glutaraldehyde of these enzymes on chitosan beads resulted in a significant stabilization of the amine transaminases investigated.</p> </abstract>