Purification and Characterization of Wheat Protein Disulfide Isomerase Expressed in <i>Escherichia coli</i>

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  • ARAI Satomi
    Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture
  • NOGUCHI Tomohiro
    Food Processing Center, Faculty of Applied Bioscience, Tokyo University of Agriculture
  • UCHINO Masataka
    Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture
  • TAKANO Katsumi
    Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture

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Other Title
  • コムギ由来プロテインジスルフィドイソメラーゼの発現，精製と性状
  • Purification and characterization of wheat protein disulfide isomerase expressed in Escherichia coli

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<p>　A protein disulfide isomerase (PDI) coding sequence was cloned from wheat (Triticum aestivum cv 'Haruyutaka'). The cDNA contained 3 distinct sequences; 2 of them, wPDI 1 and wPDI 3, were 1548 bp in length, and the other, wPDI 2, was 1539 bp in length. Sequences wPDI 1 and wPDI 2 shared 98.6% identity, wPDI 1 and wPDI 3 shared 99.2% identity, and wPDI 2 and wPDI 3 shared 99.0% identity. The total PDI activity of recombinant (r) PDI was 114 U, and the specific activity was 336 U/mg. The rPDI catalyzed the formation of disulfide bonds in disulfide reduced and denatured ovalbumin. The optimal temperature for the 2 PDIs (rPDI and native PDI) was 35℃, and PDI activity was highest at pH 8.5. Furthermore, the rPDI was superior to the native PDI with respect to heat and pH stability; however, the rPDI and native PDI had similar optimum conditions. This study is the first to demonstrate recombinant expression of wheat PDI.</p>

Journal

  • Food Preservation Science

    Food Preservation Science 37 (4), 173-183, 2011

    Japan Association of Food Preservation Scientists

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