Effect of family 22 carbohydrate-binding module on the thermostability of Xyn10B catalytic module from Clostridium stercorarium.
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.
Araki
Rie
R
Sustainable Resource Sciences, Graduate School of Bioresources, Mie University.
Karita
Shuichi
S
Tanaka
Akiyoshi
A
Kimura
Tetsuya
T
Sakka
Kazuo
K
D001483:Base Sequence; D002152:Calorimetry, Differential Scanning; D050260:Carbohydrate Metabolism; D002384:Catalysis; D017931:DNA Primers; D043364:Endo-1,4-beta Xylanases / Q000378:metabolism*; D004795:Enzyme Stability
D017931:DNA Primers; D043364:Endo-1,4-beta Xylanases