Immobilization of two (R)-Amine Transaminases on an Optimized Chitosan Support for the Enzymatic Synthesis of Optically Pure Amines

被引：28

作者：

Mallin, Hendrik ^{[1
]}

Menyes, Ulf ^{[2
]}

Vorhaben, Torge ^{[3
]}

Hoehne, Matthias ^{[4
]}

Bornscheuer, Uwe T. ^{[1
]}

机构：

[1] Ernst Moritz Arndt Univ Greifswald, Inst Biochem, Dept Biotechnol & Enzyme Catalysis, D-17487 Greifswald, Germany

[2] Enzymicals AG, D-17489 Greifswald, Germany

[3] Neoplas GmbH, D-17489 Greifswald, Germany

[4] Ernst Moritz Arndt Univ Greifswald, Inst Biochem, D-17487 Greifswald, Germany

来源：

CHEMCATCHEM | 2013年 / 5卷 / 02期

关键词：

asymmetric synthesis; chitosan beads; enzyme catalysis; immobilization; transaminase; ASYMMETRIC-SYNTHESIS;

D O I：

10.1002/cctc.201200420

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

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 -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.

引用

页码：588 / 593

页数：6