• Title of article

    NOTE: Identification of Wheat Protein Components Involved in Polymer Formation on Incubation with Transglutaminase.

  • Author/Authors

    Mujoo، . نويسنده , , Ng، P. K. W. نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2003
  • Pages
    -702
  • From page
    703
  • To page
    0
  • Abstract
    Transglutaminase (TG) catalyzes acyl-transfer reactions, introducing covalent cross-links between L-lysine and L-glutamine residues. As a result, peptides are connected and the structure of a stabilized protein network is formed, thereby improving protein strength. In this study, wheat flour was incubated with TG for different time intervals (0, 30, 60, 120, and 240 min) and the extent of polymer formation and proteins involved were investigated by SE-HPLC, SDS-PAGE, and RP-HPLC. Results indicated that the amount of polymers formed increased with incubation time. TG induced the cross-linking of HMW glutenin subunits more so than of other proteins in wheat
  • Keywords
    Cocos nucifera , peat substitutes , container media , waste-grade coir , Sustainable Agriculture , waste reclamation
  • Journal title
    CEREAL CHEMISTRY
  • Serial Year
    2003
  • Journal title
    CEREAL CHEMISTRY
  • Record number

    78492