标题:Kinetic resolution of 2-hydroxybutanoate racemic mixtures by NAD-independent l-lactate dehydrogenase
作者:Gao, C.;Zhang, W.;Ma, C.;Liu, P.;Xu, P.
作者机构:[Gao, C] State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China, MOE Key Laboratory of Microbial Metabolism and School 更多
通讯作者:Ma, C
通讯作者地址:[Xu, P]Shanghai Jiao Tong Univ, Sch Life Sci & Biotechnol, Shanghai 200240, Peoples R China.
来源:Bioresource Technology: Biomass, Bioenergy, Biowastes, Conversion Technologies, Biotransformations, Production Technologies
出版年:2011
卷:102
期:7
页码:4595-4599
DOI:10.1016/j.biortech.2011.01.003
关键词:2-Oxobutanoate;D-2-Hydroxybutanoate;Ion exchange;Kinetic resolution;NAD-Independent l-lactate dehydrogenase
摘要:Optically active d-2-hydroxybutanoate is an important building block intermediate for medicines and biodegradable poly(2-hydroxybutanoate). Kinetic resolution of racemic 2-hydroxybutanoate may be a green and desirable alternative for d-2-hydroxybutanoate production. In this work, d-2-hydroxybutanoate at a high concentration (0.197. M) and a high enantiomeric excess (99.1%) was produced by an NAD-independent l-lactate dehydrogenase (l-iLDH) containing biocatalyst. 2-Oxobutanoate, another important intermediate, was co-produced at a high concentration (0.193. M). Using a simple ion exchange process with the macroporous anion exchange resin D301, d-2-hydroxybutanoate was separated from the biotransformation system with a high recovery of 84.7%.
收录类别:EI;SCOPUS;SCIE
WOS核心被引频次:17
Scopus被引频次:20
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-79951944792&doi=10.1016%2fj.biortech.2011.01.003&partnerID=40&md5=286a8407072ee73514cfe0df7fcb4b9d
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