Purification and properties of agarase from Pseudomonas sp. PT-5

DOI 被引用文献12件

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  • Purification and Some Properties of Agarase from Pseudomonas sp. PT-5.

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An agarase (agarose 4-glycanohydrolase, EC 3.2.1.81) was purified from the culture fluid of Pseudomonas sp. PT-5 by ammonium sulfate precipitation followed by Cellulofine GC-700m, Hydroxyapatite, Butyl-Toyopearl 650M, and Toyopearl-HW 508 column chromatography. The purified enzyme gave a single band on polyacrylamide gel disc electrophoresis and its molecular weight was 31, 000 by SDS-polyacrylamide gel electrophoresis. The isoelectric point of the enzyme was 3.6. The amino-terminal sequence was H•Ala-Asp-Trp-Asp-Gly-Leu-Ala-Val-Pro-Ala-Asp-Ala-Gly-Asp-Gly-. The enzyme was stable from pH 6 to 9 and had its maximum activity at pH 8.5. The enzyme rapidly reduced the viscosity of agarose solution and its activity was greatly inhibited by metal ions such as Zn2+, Cu2+, Co2+, Fe2+, and Al3+ at 1 mM concentration. The enzyme activity was elevated by 75% in the presence of 0.1 M NaCl.

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詳細情報 詳細情報について

  • CRID
    1390001206463976704
  • NII論文ID
    110006325234
  • NII書誌ID
    AA00515312
  • DOI
    10.1271/bbb1961.55.2531
  • COI
    1:CAS:528:DyaK3MXmslChs7k%3D
  • ISSN
    18811280
    00021369
    http://id.crossref.org/issn/00021369
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • Crossref
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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