• Title of article

    A new support for the immobilization of penicillin acylase

  • Author/Authors

    He، نويسنده , , Jing and Li، نويسنده , , Xiaofen and Evans، نويسنده , , D.G and Duan، نويسنده , , Xue and Li، نويسنده , , Chengyue Li، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2000
  • Pages
    9
  • From page
    45
  • To page
    53
  • Abstract
    Mesoporous MCM-41 having well ordered long-range structure, large pore diameters, narrow pore-size distribution, high pore volume and specific surface area has been synthesized. The surface of MCM-41 has an abundance of weakly acidic hydroxyl groups. Assay results show that MCM-41 is a more effective support for the immobilization of Penicillin Acylase (PA) than many of other supports due to its structural and surface characteristics. PA can be immobilized on MCM-41 through either direct immobilization or covalent coupling. The former gives higher activity of IME than the later. In the direct immobilization, PA molecules are immobilized on MCM-41 through the hydrogen-bonded interaction between hydroxyl groups of MCM-41 and carbonyl or amino groups in the PA molecule.
  • Keywords
    Immobilization , MCM-41 , Penicillin acylase
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Serial Year
    2000
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Record number

    1715867