• Title of article

    Rational design of a more stable penicillin G acylase against organic cosolvent

  • Author/Authors

    Yang، نويسنده , , Sheng and Zhou، نويسنده , , Liping and Tang، نويسنده , , Haixu and Pan، نويسنده , , Jiang and Wu، نويسنده , , Xingjia and Huang، نويسنده , , He and Yuan، نويسنده , , Zhongyi، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2002
  • Pages
    6
  • From page
    285
  • To page
    290
  • Abstract
    We have used a simple and efficient approach by combining the known functional and structural properties of penicillin G acylase (PGA) from E. coli, and tried to mutate PGA of Bacillus megaterium with the goal of increasing the stability of the enzyme in organic solvents or at acidic pH. The PGA mutants Kβ427A, Kβ430A and Kβ427A/Kβ430A obtained have higher stability in DMF than the wild-type PGA.
  • Keywords
    Penicillin G acylase , protein stability , protein engineering
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Serial Year
    2002
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Record number

    1709408