title: Visualization of cellobiohydrolase I from Trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy.
abstract: Cellulases hydrolyze β-1,4-glucosidic linkages of insoluble cellulose at the solid/liquid interface, generating soluble cellooligosaccharides. We describe here our method for real-time observation of the behavior of cellulase molecules on the substrate, using high-speed atomic force microscopy (HS-AFM). When glycoside hydrolase family 7 cellobiohydrolase from Trichoderma reesei (TrCel7A) was incubated with crystalline cellulose, many enzyme molecules were observed to move unidirectionally on the surface of the substrate by HS-AFM. The velocity of the moving molecules of TrCel7A on cellulose I crystals was estimated by means of image analysis.
authors.affiliation: Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
authors.forename: Kiyohiko
authors.initials: K
authors.lastname: Igarashi
authors.forename: Takayuki
authors.initials: T
authors.lastname: Uchihashi
authors.forename: Anu
authors.initials: A
authors.lastname: Koivula
authors.forename: Masahisa
authors.initials: M
authors.lastname: Wada
authors.forename: Satoshi
authors.initials: S
authors.lastname: Kimura
authors.forename: Merja
authors.initials: M
authors.lastname: Penttilä
authors.forename: Toshio
authors.initials: T
authors.lastname: Ando
authors.forename: Masahiro
authors.initials: M
authors.lastname: Samejima
mesh_terms: D002482:Cellulose / Q000378:metabolism / Q000648:ultrastructure*; D043366:Cellulose 1,4-beta-Cellobiosidase / Q000378:metabolism / Q000648:ultrastructure*; D018625:Microscopy, Atomic Force / Q000379:methods*; D014242:Trichoderma / Q000201:enzymology*
chemical_list: D002482:Cellulose; D043366:Cellulose 1,4-beta-Cellobiosidase