紅藻α-グルカンリアーゼの性質と作用  [in Japanese] Properties and Action of α-1, 4-Glucan Lyase  [in Japanese]

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Abstract

α-Glucan lyase was purified from a seaweed, Graciralia chorda, by means of starch adsorption, ion-exchange chromatography and gel-filtration. The enzyme was stabilized and activated in the presence of Ca<SUP>2</SUP><SUP>+</SUP> and CI<SUP>-</SUP> ions. Chemical modifications showed that a carboxyl residue was essen-tial to the activity and a tryptophanyl residue(s) was probably involved in substrate binding. The enzyme degraded waxy rice amylopectin from its non-reducing ends and left the outermost chains as glucosyl residues. 1, 5-Anhydro-D-arabino-hex-2-ulose (1, 5-anhydro-D-fructose) was prepared by reacting the enzyme on waxy corn starch with 50% yields. The sugar served as an antioxidant on the oxidation of linoleic acid and its ability was -2-fold as high as that of ascorbic acid.

Journal

  • Journal of Applied Glycoscience

    Journal of Applied Glycoscience 47(2), 269-273, 2000-06-30

    The Japanese Society of Applied Glycoscience

References:  13

Codes

  • NII Article ID (NAID)
    10008252018
  • NII NACSIS-CAT ID (NCID)
    AN10453916
  • Text Lang
    JPN
  • Article Type
    REV
  • ISSN
    13403494
  • NDL Article ID
    5436155
  • NDL Source Classification
    ZP24(科学技術--化学・化学工業--糖・澱粉)
  • NDL Call No.
    Z17-15
  • Data Source
    CJP  NDL  J-STAGE 
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