Effect of Family 22 Carbohydrate-Binding Module on the Thermostability of Xyn10B Catalytic Module from<i>Clostridium stercorarium</i>

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  • ARAKI Rie
    Sustainable Resource Sciences, Graduate School of Bioresources, Mie University
  • KARITA Shuichi
    Sustainable Resource Sciences, Graduate School of Bioresources, Mie University
  • TANAKA Akiyoshi
    Lifesciences, Graduate School of Bioresources, Mie University
  • KIMURA Tetsuya
    Sustainable Resource Sciences, Graduate School of Bioresources, Mie University
  • SAKKA Kazuo
    Sustainable Resource Sciences, Graduate School of Bioresources, Mie University

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  • Effect of Family 22 Carbohydrate-Binding Module on the Thermostability of Xyn10B Catalytic Module from Clostridium stercorarium

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説明

A family 22 carbohydrate-binding module (CBM22) from Clostridium stercorarium Xylanase10B raised the optimum temperature of the xylanase, but in the remaining activity of heating test, apparently the catalytic module alone showed higher remaining activity. Differential scanning calorimetry showed that CBM22 conferred resistance to thermal unfolding of the enzyme and prevented the enzyme from refolding after thermal unfolding.

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