首页> 外文期刊>ChemCatChem >Immobilization of two (R)-Amine Transaminases on an Optimized Chitosan Support for the Enzymatic Synthesis of Optically Pure Amines
【24h】

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

机译:固定两种(R)-amine转氨酶对优化的壳聚糖载体的酶合成光学纯胺的酶促合成

获取原文
获取原文并翻译 | 示例
获取外文期刊封面目录资料

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.
机译:将来自Gibberella Zeae(Gibzea)和NeoSartoryaFischeri(Neofis)的两种(R)选择胺转氨酶固定在壳聚糖作为载体中以改善其在生物催化合成的手性(R) - 胺中的应用。 使用来自vibrio fluvialis(VFTA)的(S)的选择酶进行比较。 在改善固定条件后,所有酶可以有效地固定。 另外,可以提高Gibzea和Neofis的热稳定性,并且对于Gibzea,观察到pH值的略微偏移。 所有酶在 - 甲基苄胺的转化中显示出良好的活性。 在来自相应的酮的(R)-2-氨基己烷的不对称合成中,与游离酶相比,对固定的Gibzea发现了13.4倍的转化率(> 99%)。 因此,与壳聚糖珠粒上这些酶的戊二醛的共价结合导致研究胺转氨酶的显着稳定性。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号