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Tavagnacco, L., Mason, P.E., Schnupf, U., Pitici, F., Zhong, L., Himmel, M.E., Crowley, M., Cesaro, A. and Brady, J.W. (2011) Sugar-binding sites on the surface of the carbohydrate-binding module of CBH I from Trichoderma reesei. Carbohydrate Research, 346, 839-846.
http://dx.doi.org/10.1016/j.carres.2011.01.019

has been cited by the following article:

• TITLE: Evolution and impact of cellulose architecture during enzymatic hydrolysis by fungal cellulases

  AUTHORS: Marie Chauve, Loic Barre, Sandra Tapin-Lingua, Denilson da Silva Perez, Dominique Decottignies, Serge Perez, Nicolas Lopes Ferreira

  KEYWORDS: Cellulose; Cellulase; Trichoderma reesei; Synchrotron X-Ray Scattering; Neutron Scattering; Particle Size

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.12, December 27, 2013

  ABSTRACT: The enzymatic hydrolysis of cellulose is still considered as a main limiting step of the biological production of biofuels from ligno-cellulosic biomass. Glycoside hydrolases from Trichoderma reesei are currently used to produce fermentable glucose units from degradation of cellulose packed in a complex assembly of cellulose microfibrils. The present work describes the structural evolution of two prototypical samples of cellulose (a micro-crystalline cellulose and a bleached sulfite pulp) over 5 length scale orders of magnitude. The results were obtained through wide angle, small angle and ultra-small angles synchrotron X-ray scattering, completed by Small Angle Neutron Scattering and particle size analyzers. These structural evolutions were followed as a function of enzymatic conversion. The results show that whereas there is no change at the nanometer scale, drastic changes occur at micron. The observed decrease of the size of the cellulose particles is accompanied by a smoothing of the crystalline surfaces that can be explained by a two-step mechanism of the enzymatic hydrolysis.