Characterization of d-lactate dehydrogenase from Pediococcus acidilactici that converts phenylpyruvic acid into phenyllactic acid

被引:0
作者
Wanmeng Mu
Shuhuai Yu
Bo Jiang
Xingfeng Li
机构
[1] Jiangnan University,State Key Laboratory of Food Science and Technology
[2] Hebei University of Science and Technology,College of Bioscience and Bioengineering
来源
Biotechnology Letters | 2012年 / 34卷
关键词
-Lactate dehydrogenase; 3-Phenyllactic acid; Phenylpyruvic acid;
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摘要
The gene coding for d-lactate dehydrogenase (d-LDH) from Pediococcus acidilactici DSM 20284 was cloned and expressed in E. coli. The recombinant enzyme was purified by nickel-affinity chromatography. It converted phenylpyruvic acid (PPA) to 3-phenyllactic acid maximally at 30°C and pH 5.5 with a specific activity of 140 and 422 U/mg for PPA and pyruvate, respectively. The Km, turnover number (kcat), and catalytic efficiency (kcat/Km) for PPA were 2.9 mM, 305 s−1, and 105 mM−1 s−1, respectively.
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页码:907 / 911
页数:4
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