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

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Abstract

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 K m, turnover number (k cat), and catalytic efficiency (k cat/K m) for PPA were 2.9 mM, 305 s−1, and 105 mM−1 s−1, respectively.

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Acknowledgments

This work was supported by the 973 Project (No. 2012CB720802), NSFC Project (No. 31171705 and 20906040), the 863 Project (No. 2011AA100904), the Support Project of Jiangsu Province (No. BE2010678 and BE2010626), and the Open Project Program of State Key Laboratory of Food Science and Technology, Jiangnan University (No. SKLF-KF-201105).

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Authors and Affiliations

  1. State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, Jiangsu, China

    Wanmeng Mu, Shuhuai Yu, Bo Jiang & Xingfeng Li

  2. College of Bioscience and Bioengineering, Hebei University of Science and Technology, Shijiazhuang, 050018, China

    Xingfeng Li

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  1. Wanmeng Mu
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  2. Shuhuai Yu
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Correspondence to Wanmeng Mu.

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Mu, W., Yu, S., Jiang, B. et al. Characterization of d-lactate dehydrogenase from Pediococcus acidilactici that converts phenylpyruvic acid into phenyllactic acid. Biotechnol Lett 34, 907–911 (2012). https://doi.org/10.1007/s10529-012-0847-1

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  • DOI: https://doi.org/10.1007/s10529-012-0847-1

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