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

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概要

• 論文の詳細を見る

• 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.

• 社団法人 日本農芸化学会の論文
• 2006-12-23

著者

• Araki T

  Faculty Of Bioresources Mie University

• Arai Takamitsu

  Faculty Of Bioresources And Center For Molecular Biology And Genetics Mie University

• Kajino T

  Special Research Laboratory Ii Toyota Central R&d Laboratories Inc.

• Kimura Tetsuya

  National Center For Seeds And Seedlings

• Aburatani Takeshi

  Faculty Of Bioresources Mie University

• Sakka K

  Graduate School Of Bioresources Mie Univ.

• Kimura Tetsuya

  Department Of Science Kobe University

• Arai T

  National Inst. Of Fruit Tree Sci. Nagasaki Jpn

• Karita S

  Graduate School Of Regional Innovation Studies Mie Univ.

• 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

• Kimura Tetsuya

  Graduate School Of Bioresources Mie University

• Araki Rie

  Sustainable Resource Sciences Graduate School Of Bioresources Mie University

• Kitahashi T

  Brain-operative Expression Laboratory Brain Science Institute

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