Binding of Thermobifida fusca CDCel5A, CDCel6B and CDCel48A to easily hydrolysable and recalcitrant cellulose fractions on BMCC

This publication has 31 references indexed in Scilit:

• Widely different off rates of two closely related cellulose‐binding domains from Trichoderma reesei
  European Journal of Biochemistry, 1999
• The roles and function of cellulose-binding domains
  Journal of Biotechnology, 1997
• The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose.
  Proceedings of the National Academy of Sciences, 1996
• Cellulose morphology and enzymatic reactivity: A modified solute exclusion technique
  Biotechnology and Bioengineering, 1994
• Comparison of pretreatment methods on the basis of available surface area
  Bioresource Technology, 1992
• Structural and functional domains of cellobiohydrolase I from trichoderma reesei
  European Biophysics Journal, 1988
• Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei
  FEBS Letters, 1986
• The Effect of Pore Size Distribution on the Rate of Enzymatic Hydrolysis of Cellulosic Substrates
  Bio/Technology, 1985
• Mechanism of the enzymatic hydrolysis of cellulose: Effects of major structural features of cellulose on enzymatic hydrolysis
  Biotechnology and Bioengineering, 1980
• Digestibility as a Simple Function of a Molecule of Similar Size to a Cellulase Enzyme
  1969