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Production of 3-hydroxypropionic acid from glycerol by recombinant Pseudomonas denitrificans

Authors

  • Shengfang Zhou,

    1. Department of Chemical and Biomolecular Engineering, Pusan National University, Busan, Republic of Korea
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  • Christy Catherine,

    1. Department of Chemical and Biomolecular Engineering, Pusan National University, Busan, Republic of Korea
    2. Department of Fine Chemical Engineering and Applied Chemistry, Chungnam National University, Daejeon, Republic of Korea
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  • Chelladurai Rathnasingh,

    1. Department of Chemical and Biomolecular Engineering, Pusan National University, Busan, Republic of Korea
    2. Research and Development Center, GS Caltex Corporation, Daejeon, Republic of Korea
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  • Ashok Somasundar,

    1. Department of Chemical and Biomolecular Engineering, Pusan National University, Busan, Republic of Korea
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  • Sunghoon Park

    Corresponding author
    1. Department of Chemical and Biomolecular Engineering, Pusan National University, Busan, Republic of Korea
    • Correspondence to: S. Park

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  • Shengfang Zhou and Christy Catherine contributed equally to this work.

ABSTRACT

3-Hydroxypropionic acid (3-HP) can be produced from glycerol through two sequential enzymatic reactions that are catalyzed by a coenzyme B12-dependent glycerol dehydratase and an NAD(P)+-dependent aldehyde dehydrogenase (ALDH), respectively. Pseudomonas denitrificans synthesizes coenzyme B12 under aerobic conditions, where NAD(P)+ is regenerated efficiently. Hence, it is considered an ideal host for the production of 3-HP from glycerol under aerobic conditions. In this study, recombinant strains of P. denitrificans were developed and their potential for the production of 3-HP from glycerol was evaluated. When the enzymes, glycerol dehydratase (DhaB) and glycerol dehydratase reactivase (GdrAB), of Klebsiella pneumoniae were expressed heterologously, P. denitrificans could produce 3-HP at 37.7 mmol/L with 62% (mol/mol) yield on glycerol. Glucose was required as the carbon and energy sources for cell growth. The overexpression of heterologous ALDH was not essential; however, the titer and yield of 3-HP were improved to 54.7 mmol/L and 67% (mol/mol), respectively, when an ALDH gene (puuC) from K. pneumoniae was overexpressed. One serious drawback hindering the use of P. denitrificans as a recombinant host for 3-HP production is that it oxidizes 3-HP to malonate and utilizes 3-HP as a carbon source for growth. This is the first report on the development and use of recombinant P. denitrificans for 3-HP production from glycerol. Biotechnol. Bioeng. 2013;110: 3177–3187. © 2013 Wiley Periodicals, Inc.

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