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