• Title/Summary/Keyword: extracellular pullulan 6-glucanohydrolase (EP)

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Biochemical characterization of a novel extracellular pullulan 6-glucanohydrolase from Bacillus circulans S-1

  • Lee, Moon-Jo;Park, Cheon;Park, Joon-Ho;Chung, Kang-Hyun;Nam, Kyung-Soo;Park, Jin-Woo;Kim, Cheorl-Ho
    • Journal of Life Science
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    • v.10 no.3
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    • pp.307-316
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    • 2000
  • Bacillus circulans S-1 extracellular pullulan 6-glucanohydrolase (EP) (EC 3.2.1.41) has been characterized with a purified enzyme of 140 kDa. The N-terminal amino acid sequence of the purified enzyme was P-L-N-M-S-Q-P. The enzyme displayed a temperature optimum of around $60^{\circ}C$ and a pH optimum of around pH 9.0. The enzyme was stable to incubation from pH 4.0 to pH 11.0 at $4^{\circ}C$ for 48h. The presence of substrate allowed the protection of the enzyme from heat inactivation. The activity of the enzyme was stimulated by several metal ions such as Mn2+ and Ca2+. The enzyme had an apparent Km of 7.92 mg/ml for pullulan. The purfied enzyme completely hydrolysed pullulan to maltotriose.

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