• Title of article

    NMR spectroscopy analysis of oligoguluronates and oligomannuronates prepared by acid or enzymatic hydrolysis of homopolymeric blocks of alginic acid. Application to the determination of the substrate specificity of Haliotis tuberculata alginate lyase

  • Author/Authors

    Alain Heyraud، نويسنده , , Claude Gey، نويسنده , , Christine Leonard، نويسنده , , Cyril Rochas، نويسنده , , Sylvie Girond، نويسنده , , Bernard Kloareg، نويسنده ,

  • Issue Information
    دوهفته نامه با شماره پیاپی سال 1996
  • Pages
    13
  • From page
    11
  • To page
    23
  • Abstract
    The 1H and 13C NMR chemical shifts of the various saturated and unsaturated trimers obtained by acid or enzymatic depolymerisation of homopolymeric blocks of alginates are reported. In addition, 13C NMR chemical shifts are assigned for several saturated oligomers of higher polymerisation degrees. Breakdown of alginate and of homopolymeric alginate blocks by Haliotis tuberculata alginate lyase was monitored with 1H NMR spectroscopy and the signals relevant to the identification of the lyase products are pointed out. The enzyme performs β-elimination on the mannuronic acid residues, independently of their immediately surrounding neighbours. Application of this approach to the analysis of the substrate specificity of alginate lyases is discussed.
  • Keywords
    NMR , Oligomannuronates , Alginic acid , substrate specificity , Haliotis tuberculata , Alginate lyase , Oligoguluronates
  • Journal title
    Carbohydrate Research
  • Serial Year
    1996
  • Journal title
    Carbohydrate Research
  • Record number

    961489