• Title/Summary/Keyword: DfAIII

Search Result 1, Processing Time 0.017 seconds

Purification and Properties of Inulase II from Arthrobacter ureafaciens KCTC 3387 (Arthrobacter ureafaciens KCTC 3387이 생산하는 Inulase II의 정제 및 특성)

  • 이재찬;이기영;송기방;이용복
    • Microbiology and Biotechnology Letters
    • /
    • v.27 no.6
    • /
    • pp.471-476
    • /
    • 1999
  • Inulin fructotransferase(depolymerizing)(EC 2.4.1.93)(inulaseII) which converts inulin into di-D-fructofuranose-1,2':2,3'-dianhydride (DFAIII) was purified from Arthrobacter ureafaciens KCTC 3387 using column chromatography on DEAE-Toyopearl 650M and gel filtration of Sephadex G-200. The enzyme was purified 7-fold with a yield of 11% from a culture supernatant. The purified enzyme gave a single band on polyacrylamide gel electrophoresis, and the molecular weight of the enzyme was estimated to be 45,000 by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the enzyme reaction were pH6.5~7.0 and $55{\circ}C$, respectively. The enzyme was stable within a pH range of 5.0 to 10.6 and up to $60^{\circ}C$. The Km of this enzyme for DFAIII production was 11.9mM. The enzyme was inactivated by $Hg^{2+}$ and after exhaustive digestion of inulin by this enzyme, 1-kestose and nystose were produced in addition of DFAIII.

  • PDF