Propioin synthesis using thiamine diphosphate‐dependent enzymes
Propioin synthesis using thiamine diphosphate‐dependent enzymes
复制标题
使用二磷酸硫胺素依赖性酶合成丙酸
DOI：
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发表时间：
2009
期刊：
影响因子：
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通讯作者：
J. Büchs
中科院分区：
文献类型：
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作者：
R. Mikolajek;A. Spiess;M. Pohl;J. Büchs
来自荧光假单胞菌的苯甲醛裂解酶（BAL，EC 4.1.2.38）和来自恶臭假单胞菌的苯甲酰甲酸脱羧酶（BFD，EC4.1.1.7）是硫胺素二磷酸依赖性酶。这些酶具有共同的四聚体结构，并催化各种C → C →键形成和断裂反应。本文详细研究了在间歇式反应器中，以BAL或BFD为催化剂，水溶液为反应介质，由丙醛不对称合成丙酸甘油酯的反应。两种酶在高浓度丙醛存在下失活。与BAL相比，BFD在反应条件下以及储存期间更稳定。动力学研究显示，BAL具有典型的Michaelis-Menten动力学，最大比反应速率为26.2 U/mg，KM异常高，为415 mM，而BFD的v/[S]-曲线在研究的浓度范围内（100-1500 mM）几乎呈线性。两种酶都产生具有相反对映体过量的丙炔酸：BAL产生（S）-丙炔酸（ee为35%），而BFD产生（R）-对映体（ee为67%）。© 2009年美国化学工程师学会生物技术。程序，2009
Benzaldehyde lyase (BAL, EC 4.1.2.38) from Pseudomonas fluorescens and benzoylformate decarboxylase (BFD, EC 4.1.1.7) from Pseudomonas putida are thiamine diphosphate‐dependent enzymes. These enzymes share a common tetrameric structure and catalyze various CC‐bond forming and breaking reactions. Here we describe a detailed study of the asymmetric synthesis of propioin from propanal catalyzed by BAL or BFD in aqueous solution in a batch reactor. Both enzymes are deactivated in the presence of high concentration of propanal. Compared to BAL, BFD is more stable under reaction conditions as well as during storage. The kinetic studies showed a typical Michaelis‐Menten kinetic for BAL with a maximal specific reaction rate of 26.2 U/mg and an unusually high KM of 415 mM, whereas the v/[S]‐plot for BFD is almost linear in the concentration range (100–1500 mM) investigated. Both enzymes produce propioin with opposite enantiomeric excess: BAL produced the (S)‐propioin (ee of 35%), whereas BFD yielded the (R)‐enantiomer (ee of 67%). © 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009
影响因子：
2.9
作者：
Hasson, MS;Muscate, A;Ringe, D
通讯作者：
Ringe, D