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

Biosci Biotechnol Biochem. 2006 Dec;70(12):3039-41. doi: 10.1271/bbb.60348. Epub 2006 Dec 7.

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.

MeSH terms

  • Base Sequence
  • Calorimetry, Differential Scanning
  • Carbohydrate Metabolism*
  • Catalysis
  • DNA Primers
  • Endo-1,4-beta Xylanases / metabolism*
  • Enzyme Stability

Substances

  • DNA Primers
  • Endo-1,4-beta Xylanases