title: The use of carbohydrate binding modules (CBMs) to monitor changes in fragmentation and cellulose fiber surface morphology during cellulase- and Swollenin-induced deconstruction of lignocellulosic substrates.
abstract: Although the actions of many of the hydrolytic enzymes involved in cellulose hydrolysis are relatively well understood, the contributions that amorphogenesis-inducing proteins might contribute to cellulose deconstruction are still relatively undefined. Earlier work has shown that disruptive proteins, such as the non-hydrolytic non-oxidative protein Swollenin, can open up and disaggregate the less-ordered regions of lignocellulosic substrates. Within the cellulosic fraction, relatively disordered, amorphous regions known as dislocations are known to occur along the length of the fibers. It was postulated that Swollenin might act synergistically with hydrolytic enzymes to initiate biomass deconstruction within these dislocation regions. Carbohydrate binding modules (CBMs) that preferentially bind to cellulosic substructures were fluorescently labeled. They were imaged, using confocal microscopy, to assess the distribution of crystalline and amorphous cellulose at the fiber surface, as well as to track changes in surface morphology over the course of enzymatic hydrolysis and fiber fragmentation. Swollenin was shown to promote targeted disruption of the cellulosic structure at fiber dislocations.
authors.affiliation: From the Forest Products Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada and.
authors.forename: Keith
authors.initials: K
authors.lastname: Gourlay
authors.affiliation: From the Forest Products Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada and.
authors.forename: Jinguang
authors.initials: J
authors.lastname: Hu
authors.affiliation: From the Forest Products Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada and.
authors.forename: Valdeir
authors.initials: V
authors.lastname: Arantes
authors.affiliation: the VTT Technical Research Centre of Finland, Metallimiehenkuja 2 (Espoo), FI-02044 VTT, Finland.
authors.forename: Merja
authors.initials: M
authors.lastname: Penttilä
authors.affiliation: From the Forest Products Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada and jack.saddler@ubc.ca.
authors.forename: Jack N
authors.initials: JN
authors.lastname: Saddler
mesh_terms: D002480:Cellulase / Q000378:metabolism*; D002482:Cellulose / Q000737:chemistry* / Q000378:metabolism*; D008031:Lignin / Q000737:chemistry* / Q000378:metabolism*; D018613:Microscopy, Confocal; D011485:Protein Binding; D014961:X-Ray Diffraction
chemical_list: C036909:lignocellulose; D002482:Cellulose; D008031:Lignin; D002480:Cellulase
keywords: Amorphogenesis; Carbohydrate Binding Modules (CBMs); Cellulase; Cellulose; Cellulose Binding Modules; Confocal Microscopy; Enzyme; Fiber Dislocations; Fragmentation; Fungi; Microbiology; Swollenin