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Cloning, Expression, and Characterization of Bacillus sp. Snu-7 Inulin Fructotransferase

Kim, Chung-Sei ; Hong, Chang-Ki ; Kim, Kyoung-Yun ; Wang, Xiu-Ling ; Kang, Su-Il ; Kim, Su-Il

Journal of Microbiology and Biotechnology, 2007, 17(1), , pp.37-43 [Periódico revisado por pares]

한국미생물생명공학회

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  • Título:
    Cloning, Expression, and Characterization of Bacillus sp. Snu-7 Inulin Fructotransferase
  • Autor: Kim, Chung-Sei ; Hong, Chang-Ki ; Kim, Kyoung-Yun ; Wang, Xiu-Ling ; Kang, Su-Il ; Kim, Su-Il
  • Assuntos: Bacillus sp. snu-7 ; difructofuranose anhydride ; inulin fructotransferase ; 생물학
  • É parte de: Journal of Microbiology and Biotechnology, 2007, 17(1), , pp.37-43
  • Notas: The Korean Society for Applied Microbiology
    KISTI1.1003/JNL.JAKO200708506317805
    G704-000169.2007.17.1.009
  • Descrição: A gene encoding inulin fructotransferase (di-D-fructofuranose 1,2': 2,3' dianhydride [DFA III]-producing IFTase, EC 4.2.2.18) from Bacillus sp. snu-7 was cloned. This gene was composed of a single, 1,353-bp open reading frame encoding a protein composed of a 40-amino acid signal peptide and a 410-amino acid mature protein. The deduced amino acid sequence was 98% identical to Arthrobacter globiformis C11-1 IFTase (DFA III-producing). The enzyme was successfully expressed in E. coli as a functionally active, His-tagged protein, and it was purified in a single step using immobilized metal affinity chromatography. The purified enzyme showed much higher specific activity (1,276 units/mg protein) than other DFA III-producing IFTases. The recombinant and native enzymes were optimally active in very similar pH and temperature conditions. With a 103-min half-life at $60^{\circ}C$, the recombinant enzyme was as stable as the native enzyme. Acidic residues and cysteines potentially involved in the catalytic mechanism are proposed based on an alignment with other IFTases and a DFA IIIase.
  • Editor: 한국미생물생명공학회
  • Idioma: Coreano
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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