• Title of article

    On the inactivity of Candida antartica lipase B towards strong acids

  • Author/Authors

    Hollmann، نويسنده , , F. and Grzebyk، نويسنده , , P. and Heinrichs، نويسنده , , V. and Doderer، نويسنده , , K. and Thum، نويسنده , , O.، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2009
  • Pages
    5
  • From page
    257
  • To page
    261
  • Abstract
    Candida antarctica lipase B (CalB, Novozyme 435) was evaluated as catalyst for the conversion of so-called edible acids (e.g. malic and tartaric acid). While transesterification using these acyl donors proceeds smoothly, albeit with low regioselectivity, esterification is hardly catalyzed. or reason for CalB inactivation the high acidity of edible acids was identified leading to irreversible inactivation of the biocatalyst. Furthermore, indication exist that all acids exhibiting a pKa value below 4.8 cause irreversible inactivation of CalB.
  • Keywords
    enzyme catalysis , Enzyme inactivation , Esterification , Lipases
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Serial Year
    2009
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Record number

    1713749