Published: December 23, 2006Received: June 22, 2006Available on J-STAGE: -Accepted: August 17, 2006
Advance online publication: December 07, 2006
Revised: -
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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