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Immobilization of two ( R )‐Amine Transaminases on an Optimized Chitosan Support for the Enzymatic Synthesis of Optically Pure Amines
Author(s) -
Mallin Hendrik,
Menyes Ulf,
Vorhaben Torge,
Höhne Matthias,
Bornscheuer Uwe T.
Publication year - 2013
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201200420
Subject(s) - glutaraldehyde , chitosan , immobilized enzyme , chemistry , amine gas treating , biocatalysis , enzyme , thermal stability , combinatorial chemistry , nuclear chemistry , organic chemistry , catalysis , reaction mechanism
Two ( R )‐selective amine transaminases from Gibberella zeae (GibZea) and from Neosartorya fischeri (NeoFis) were immobilized on chitosan as a carrier to improve their application in the biocatalytic synthesis of chiral ( R )‐amines. An ( S )‐selective enzyme from Vibrio fluvialis (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 ( R )‐2‐aminohexane from the corresponding ketone, a 13.4‐fold higher conversion (>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.