[1]任红,郭敏杰,霍鹤宇,等.固定化双酶耦联体系制备手性胺[J].深圳大学学报理工版,2019,36(No.5(473-600)):354-360.[doi:10.3724/SP.J.1249.2019.04354]
 REN Hong,GUO Minjie,HUO Heyu,et al.Biosynthesis of chiral amines with immobilized double enzyme system[J].Journal of Shenzhen University Science and Engineering,2019,36(No.5(473-600)):354-360.[doi:10.3724/SP.J.1249.2019.04354]
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固定化双酶耦联体系制备手性胺()
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《深圳大学学报理工版》[ISSN:1000-2618/CN:44-1401/N]

卷:
第36卷
期数:
2019年No.5(473-600)
页码:
354-360
栏目:
【生物工程】
出版日期:
2019-09-30

文章信息/Info

Title:
Biosynthesis of chiral amines with immobilized double enzyme system
作者:
任红1郭敏杰1霍鹤宇1姚光晓1王世珍12
1)厦门大学化学化工学院,福建厦门361005; 2)厦门市合成生物学重点实验室,福建厦门 310065
Author(s):
REN Hong1 GUO Minjie1 HUO Heyu1 YAO Guangxiao1 and WANG Shizhen12
1) College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, Fujian Province, P.R.China 2) The Key Lab for Synthetic Biotechnology of Xiamen City, Xiamen 361005, Fujian Province, P.R.China
关键词:
生物催化胺脱氢酶甲酸脱氢酶手性胺双酶耦联体系固定化酶聚乙烯亚胺
Keywords:
biocatalysis amine dehydrogenase (AmDH) formate dehydrogenase (FDH) chiral amine double enzyme coupling system immobilized enzyme polyethylenimine (PEI)
分类号:
Q814
DOI:
10.3724/SP.J.1249.2019.04354
文献标志码:
A
摘要:
胺脱氢酶(amine dehydrogenase, AmDH)能够在辅酶的作用下不对称还原前手性酮制备手性胺,并与甲酸脱氢酶(formate dehydrogenase, FDH)构建耦联双酶反应体系,通过酶活检测与高效液相色谱法得出, AmDH和FDH浓度比为4∶1、底物浓度为10 mmol/L、辅酶浓度为0.025 mmol/L时,是游离双酶耦联体系最优反应条件.为提高双酶耦联体系的稳定性,将聚乙烯亚胺-双酶复合物作为模板和催化剂,诱导钛前驱体Ti-BALDH(titanium(IV)bis-(ammoniumlactato)-dihydroxide)缩聚,形成固定化耦联体系.与游离酶体系相比,辅酶可在固定化酶体系的微环境中高效循环再生,大大提高了多酶耦联体系的催化效率.
Abstract:
Amine dehydrogenase (AmDH) can synthesize chiral amines by asymmetric reduction of prochiral ketones with coenzyme and establish a coupled double enzyme reaction system with formate dehydrogenase (FDH). The results of enzyme activity detection and high performance liquid chromatography show that the optimal reaction condition is that the concentration ratio of AmDH to FDH is 4∶1 and the concentration of substrate and the concentration of coenzyme are 10 mmol/L and 0.025 mmol/L, respectively. In order to improve the stability of the system, the polyethylenimine (PEI) coating on the enzyme surface to form polyethyleneimine-diphenylase complex as the template and catalyst was employed for the condensation of Ti-BALDH to form immobilized double enzyme coupling system. Compared with the free double enzyme system, the coenzyme can be recycled and regenerated efficiently in the microenvironment of the immobilized enzyme system. It greatly improves the catalytic efficiency of the multi-enzyme coupling system.

相似文献/References:

[1]刘森林.桃仁醇腈酶促不对称合成含硅(R)-酮氰醇[J].深圳大学学报理工版,2011,28(No.1(001-095)):54.
 LIU Sen-lin.Asymmetric synthesis of silicon containing (R)-ketone cyanhydrin catalyzed by (R)-hydroxynitrile lyase from peach seed meal[J].Journal of Shenzhen University Science and Engineering,2011,28(No.5(473-600)):54.

更新日期/Last Update: 2019-07-04