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

共 5 条

[1] Immobilization of (R)- and (S)-amine transaminases on chitosan support and their application for amine synthesis using isopropylamine as donor
Mallin, H.
Hoehne, M.
Bornscheuer, U. T.
JOURNAL OF BIOTECHNOLOGY, 2014, 191 : 32 - 37
[2] Enzymatic Asymmetric Synthesis of Enantiomerically Pure Aliphatic, Aromatic and Arylaliphatic Amines with (R)-Selective Amine Transaminases
Schaetzle, Sebastian
Steffen-Munsberg, Fabian
Thontowi, Ahmad
Hoehne, Matthias
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Bornscheuer, Uwe T.
ADVANCED SYNTHESIS & CATALYSIS, 2011, 353 (13) : 2439 - 2445
[3] Asymmetric Synthesis of Optically Pure Pharmacologically Relevant Amines Employing ω-Transaminases
Koszelewski, Dominik
Lavandera, Ivan
Clay, Dorina
Rozzell, David
Kroutil, Wolfgang
ADVANCED SYNTHESIS & CATALYSIS, 2008, 350 (17) : 2761 - 2766
[4] How to identify and characterize novel transaminases? Two novel transaminases with opposite enantioselectivity for the synthesis of optically active amines
Gal, Cristian Andrei
Barabas, Laura-Edit
Varga, Andrea
Csuka, Pal
Bencze, Laszlo Csaba
Tosa, Monica Ioana
Poppe, Laszlo
Paizs, Csaba
MOLECULAR CATALYSIS, 2022, 531
[5] Chitosan functionalized with EDTA as a new support for enzyme immobilization and its application on enzymatic resolution of (R, S)-1-phenylethanol
Magalhaes, Renata R.
Abrantes, Paloma G.
Abrantes, Poliana G.
Costa, Israel F.
Teotonio, Ercules E. S.
Vale, Juliana A.
PROCESS BIOCHEMISTRY, 2025, 149 : 128 - 136

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