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Purification and Characterization of an Intracellular Inulinase from Bacillus sphaericus 188-1

  • Kim, Jae-Ho (Department of Genetic Engineering and Bio-Med. RRC, Paichai University) ;
  • Kwak, Yoon-Jin (Department of Genetic Engineering and Bio-Med. RRC, Paichai University) ;
  • Lee, Jong-Tae (Central Research Institute, Korea Tabacco and Ginseng Corporation) ;
  • Park, Shin-Yang (Korea Food Research Institute) ;
  • Lee, Jong-Soo (Department of Genetic Engineering and Bio-Med. RRC, Paichai University)
  • Published : 2002.12.01

Abstract

In order to obtain basal data for industrial application of inulinase from Bacillus sphaeicus 188-1, its intracellular inulinase was purified by ammonium sulfate fractionation and column chromatography on DEAE-Sephadex A-50 and Sephadex G-100. The enzyme was homogeneous as judged by SDS-polyacrylamide gel electrophoresis, with an apparent molecular weight of 29 kDa. Inulinase activity was optimal at pH 6.5 and 4$0^{\circ}C$. The enzyme activity was significantly inhibited by Cu$^{2+}$, Cd$^{2+}$ and Hg$^{2+}$. The inulinase exhibited an apparent Km value of 0.014% for inulin.

Keywords

References

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