Purification and Characterization of an Isomaltotriose-producing Endo-dextranase from a Fusarium sp.

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Abstract

An isomaltotriose-producing endo-dextranase was simply purified from cell-free culture broth of a Fusarium sp. by ethanol fractionation and consecutive column chromatographibs using DEAE-Toyopearl and Bio-Gel P-100. The purified enzyme was judged to be homogeneous on PAGE and SDS-PAGE as well as isoelectric focusing. The molecular mass of the enzyme was estimated to be about 69 kDa by SDS-PAGE. The enzyme is an acidic protein with a pI of 4.6. The optimum pH and temperature were pH 6.5 and 35℃, respectively. The enzyme was completely stable over the range of pH 4.5-11.8 at 4 for 24 h and at temperatures below 45℃. Inactivation of the enzyme was found to be partial with 5 mM Cu^<2+>, being about 70% inhibition and complete with 5 mM of Fe^<3+> Hg^<2+>, Ag^+ or NBS. The enzyme split dextran in an endo-lytic action to produce a large amount of isomaltotriose and a slight amount of isomaltose rind glucose. The anomeric configurations of the reaction products formed by the enzyme were α-form, indicating that the α-glycoside linkages in the substrate are retained. The final yield of isomaltotriose from dextran T-2000 was about 62%.

Journal

Bioscience, biotechnology, and biochemistry   [List of Volumes]

Bioscience, biotechnology, and biochemistry 62(1), 117-122, 1998-01-23  [Table of Contents]

Japan Society for Bioscience, Biotechnology, and Agrochemistry

References:  22

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Codes

  • NII Article ID (NAID) :
    110002678926
  • NII NACSIS-CAT ID (NCID) :
    AA10824164
  • Text Lang :
    ENG
  • Article Type :
    Journal Article
  • ISSN :
    09168451
  • NDL Article ID :
    4406233
  • NDL Source Classification :
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL Call No. :
    Z53-G223
  • Databases :
    CJP  CJPref  NDL  NII-ELS  J-STAGE