A New Carboxylesterase from<i>Brevibacterium linens</i>IFO 12171 Responsible for the Conversion of 1,4-Butanediol Diacrylate to 4-Hydroxybutyl Acrylate: Purification, Characterization, Gene Cloning, and Gene Expression in<i>Escherichia coli</i>

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  • SAKAI Yasuyoshi
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
  • ISHIKAWA Junko
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
  • FUKASAKA Shunji
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
  • YURIMOTO Hiroya
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
  • MITSUI Ryoji
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
  • YANASE Hideshi
    Department of Biotechnology, Tottori University
  • KATO Nobuo
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University

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タイトル別名
  • A New Carboxylesterase from Brevibacterium linens IFO12171 Responsible for the Conversion of 1,4-Butanediol Diacrylate to 4-Hydroxybutyl Acrylate: Purification, Characterization, Gene Cloning, and Gene Expression in Escherichia coli.
  • New Carboxylesterase from Brevibacterium linens IFO 12171 Responsible for the Conversion of 1 4-Butanediol Diacrylate to 4-Hydroxybutyl Acrylate Purification Characterization Gene Cloning and Gene Expression in Escherichia coli

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A carboxylesterase that is responsible for conversion of 1,4-butanediol diacrylate (BDA) to 4-hydroxybutyl acrylate (4HBA) was found in Brevibacterium lines IFO 12171, and purified to homogeneity. The purified enzyme was active toward a variety of diesters of ethylene glycol, 1,4-butanediol, and 1,6-hexanediol. The Km and kcat of the enzyme for BDA were 3.04 mM and 203,000 s-1, respectively. The reaction with the purified enzyme gave 98 mM 4HBA from 100 mM BDA for 60 min.<br>   The enzyme gene was cloned from the chromosomal DNA of the bacterium. The open reading frame encoding the enzyme was 1176 bp long, corresponding to a protein of 393 amino acid residues (molecular mass=42,569 Da). The deduced amino acid sequence contained the tetra peptide motif sequence, STTK, and the serine residue was confirmed to be the catalytic center of BDA esterase by site-directed mutagenesis for several amino acid residues. The gene was expressed in Escherichia coli under the control of the lac promoter, and the gene product (a fusion protein with 6 amino acid residues from β-galactosidase) showed the same catalytic properties as the enzyme from the parent strain.<br>

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