title: Effect of family 22 carbohydrate-binding module on the thermostability of Xyn10B catalytic module from Clostridium stercorarium.
abstract: 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.
authors.affiliation: Sustainable Resource Sciences, Graduate School of Bioresources, Mie University.
authors.forename: Rie
authors.initials: R
authors.lastname: Araki
authors.forename: Shuichi
authors.initials: S
authors.lastname: Karita
authors.forename: Akiyoshi
authors.initials: A
authors.lastname: Tanaka
authors.forename: Tetsuya
authors.initials: T
authors.lastname: Kimura
authors.forename: Kazuo
authors.initials: K
authors.lastname: Sakka
mesh_terms: 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
chemical_list: D017931:DNA Primers; D043364:Endo-1,4-beta Xylanases