• Title/Summary/Keyword: (Bacillu circulans S-1)

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Bacteriophage-like Particles Induced by Mitomycin C in Bacillus circulans F-2 (Mitomycin C에 의해 유도되는 Bacillus cirulans F-2의 Bacteriophage-like 입자)

  • 김철호;권석태;이대실;타니구치하지메
    • Microbiology and Biotechnology Letters
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    • v.18 no.3
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    • pp.221-226
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    • 1990
  • To detect prophages and bacterioeins, twenty strains of Bacillus circulans were treated with mitomycin C. The resulted lysates were subjected to electron microscopy, and also examined for killing and plaque-forming activities. Fifteen strains showed killing activity on two or more strains of Bacillue circulans. Killing agents were centrifuged in linear 5 to 20% sucrose gradient, and studied with electron microscopy which revealed the presence of particles.They looked morphologically like phage tail of 190 nm long with fiber (FA9, FA5) or without fiber (FA1, FA6), T even phage-like particle with a head of 50 nm in diameter and a tail of 140 nm long (FA7), or T7 phage-like particle with a head of 70 nm in diameter and a tail of 20 nm long (FA17). The killing agent of FA17 showed phage-forming activity on several strains different from killing sensitive strains of Bacillus circulans.

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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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