VISUALIZATION OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI MOVING ON CRYSTALLINE CELLULOSE USING HIGH-SPEED ATOMIC FORCE MICROSCOPY

Kiyohiko Igarashi*, Takayuki Uchihashi, Anu Koivula, Masahisa Wada, Satoshi Kimura, Merja Penttilae, Toshio Ando, Masahiro Samejima

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterScientificpeer-review

Abstract

Cellulases hydrolyze beta-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.

Original languageEnglish
Title of host publicationCELLULASES
EditorsHJ Gilbert
PublisherACADEMIC PRESS
Pages169-182
Number of pages14
ISBN (Print)978-0-12-415931-0
DOIs
Publication statusPublished - 2012
MoE publication typeA3 Part of a book or another research book

Publication series

NameMethods in Enzymology
PublisherELSEVIER ACADEMIC PRESS INC
Volume510
ISSN (Print)0076-6879

Keywords

  • DYNAMIC BIOMOLECULAR PROCESSES
  • NEUTRON FIBER DIFFRACTION
  • HYDROGEN-BONDING SYSTEM
  • SYNCHROTRON X-RAY
  • PHANEROCHAETE-CHRYSOSPORIUM
  • ENZYMATIC-HYDROLYSIS
  • NANO-VISUALIZATION
  • SCATTERING
  • EFFICIENT
  • REVEALS

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