• Title of article

    Enzymatic properties and transglycosylation of α-galactosidase from Penicillium oxalicum SO

  • Author/Authors

    Hiroyuki and Kurakake، نويسنده , , Masahiro and Moriyama، نويسنده , , Youichirou and Sunouchi، نويسنده , , Riku and Nakatani، نويسنده , , Shinya، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2011
  • Pages
    6
  • From page
    177
  • To page
    182
  • Abstract
    Penicillium oxalicum SO α-galactosidase demonstrated weak hydrolysing activity but a high rate of transglycosylation in the reaction with melibiose, where the major product was 6-α-galactosyl melibiose. The transfer ratio was 83.6% and was maintained over a long reaction time of 80 h. The molecular weight was estimated to be 124,000 by SDS–PAGE. The optimal pH was ∼3 and a stable pH, with a range of 2.4–9.5, was found. The optimal temperature was ∼60 °C and the activity was stable below 60 °C. With respect to acceptor specificity, mono-alcohols, sugar alcohols and sugars were poor acceptors, but the di-alcohol ethylene glycol and the tri-alcohol glycerin were good acceptors. The percentage of transglycosylation to glycerin increased up to 41.7%, as that to melibiose decreased, with the initial glycerin concentration of 40%. The production of α-d-galactosylglycerol was 293 mg for each gram of melibiose used by the enzymatic reaction.
  • Keywords
    Transglycosylation Penicillium oxalicum , ?-Galactosidase , oligosaccharides , Glycerin , Melibiose
  • Journal title
    Food Chemistry
  • Serial Year
    2011
  • Journal title
    Food Chemistry
  • Record number

    1963981