• Title/Summary/Keyword: Clostridium thermocellim

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A role and properties of C/sub 1/ enriched cellulase fraction from anaerobic clostridium thermocellum in cellulose degradation (섬유소 분해시 혐기성 Clostridium thermocellum이 생산하는 Cellulase의 C/sub 1/ 성분의 역할과 성질)

  • Lee, Yong Hyeon;Sim, Uk Han;Sin, Hyeon Dong
    • Korean Journal of Microbiology
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    • v.25 no.4
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    • pp.297-297
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    • 1987
  • A $C_{1}$ enriched cellulase fraction was separated from culture filtrate of anaerobic Clostridium thermocellum by hydroxyapatite column chromatography. The separated fraction showed strong synergistic action with $C_{x}$ component (endo-$\beta$-1, 4-glucanase) in digestion of crystalline cellulose, similar to the other aerobic cellulolytic microorganisms. Unlike the $C_{x}$ component the $C_{1}$ enriched fraction was rapidly inactivated by oxidation at the atmospheric condition. The enzyme activity was significantly enhanced by the addition of reducing agents, especially $\beta$-mercaptoethanol, which indicates that a $C_{1}$ component has a lot of sulfhydryl groups essential for the enzyme activity. The effect of metal ions on $C_{1}$ activity was also investigated. The $C_{1}$ fraction was found to be thermally stable compare to endo-$\beta$-1,4-glucanase. Optimal temperature and pH were found to be 60.deg.C and 6.0, respectively.

A Role and Properties of $C_{1}$ Enriched Cellulase Fraction from Anaerobic Clostridium thermocellum in Cellulose Degradation (섬유소 분해시 혐기성 Clostridium thermocellum이 생산하는 Cellulase의 $C_{1}$ 성분의 역할과 성질)

  • 이용현;심욱한;신현동
    • Korean Journal of Microbiology
    • /
    • v.25 no.4
    • /
    • pp.293-303
    • /
    • 1987
  • A $C_{1}$ enriched cellulase fraction was separated from culture filtrate of anaerobic Clostridium thermocellum by hydroxyapatite column chromatography. The separated fraction showed strong synergistic action with $C_{x}$ component (endo-$\beta$-1, 4-glucanase) in digestion of crystalline cellulose, similar to the other aerobic cellulolytic microorganisms. Unlike the $C_{x}$ component the $C_{1}$ enriched fraction was rapidly inactivated by oxidation at the atmospheric condition. The enzyme activity was significantly enhanced by the addition of reducing agents, especially $\beta$-mercaptoethanol, which indicates that a $C_{1}$ component has a lot of sulfhydryl groups essential for the enzyme activity. The effect of metal ions on $C_{1}$ activity was also investigated. The $C_{1}$ fraction was found to be thermally stable compare to endo-$\beta$-1,4-glucanase. Optimal temperature and pH were found to be $60^{\circ}C$ and 6.0, respectively.

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