4.4 Article

Effect of family 22 carbohydrate-binding module on the thermostability of Xyn10B catalytic module from Clostridium stercorarium

Journal

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 70, Issue 12, Pages 3039-3041

Publisher

TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.60348

Keywords

carbohydrate-binding module; xylanase; thermostability; differential scanning calorimetry (DSC)

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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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