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Food science and biotechnology v.15 no.6 = no.72, 2006년, pp.908 - 913   피인용횟수: 2
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Characteristics of a Bifidobacterium longum LL04 ${\beta}$-Galactosidase (recombinant) Produced in Escherichia coli

Lim, Seong-Il   (Division of Fermented Food Research, Korea Food Research InstituteCC0186878  ); Kim, Geun-Bae   (Department of Animal Science and Technology, Chung-Ang UniversityUU0001197  ); Yi, Sung-Hun   (Department of Food Science and Agricultural Chemistry, McGill UniversityUU0015052  ); Lee, Byong-Hoon   (Department of Food Science and Agricultural Chemistry, McGill UniversityUU0015052  );
  • 초록

    Recombinant ${\beta}$ -galactosidase from Bifidobacterium longum LL04 was expressed in Escherichia coli and partially purified by ammonium sulphate precipitation and anion-exchange chromatography (Mono-Q). The optimum temperature and pH of the partially purified enzyme were $50^{\circ}C$ and pH 7.0-8.0, respectively, when o-nitrophenyl- ${\beta}$ -D-galactopyranoside was used as a substrate. The enzyme was stable over the pH range of 5.0-9.0, and was active at $40^{\circ}C$ for more than 60 min at pH 7.0. The enzyme was significantly activated by $Na^+$ and $K^+$ . Maximal activity was observed at the concentration of 10 mM for both $Na^+$ and $K^+$ . The enzyme activity was strongly inhibited by most bivalent metal ions. The Km and Vmax on ONPG at 37 and $50^{\circ}C$ were 0.72, 167.9, and 0.507 mM, 310.9 U/mL, respectively.


  • 주제어

    Bifidobacterium longum .   recombinant ${\beta}$-galactosidase .   characteristics.  

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