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 Penttilä; Toshio Ando; Masahiro Samejima

doi:10.1016/B978-0-12-415931-0.00009-4

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 Penttilä, Toshio Ando, Masahiro Samejima

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

24 Citations (Scopus)

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.

Original language	English
Title of host publication	Methods in Enzymology
Publisher	Academic Press Inc.
Pages	169-182
Number of pages	14
DOIs	https://doi.org/10.1016/B978-0-12-415931-0.00009-4
Publication status	Published - 2012

Publication series

Name	Methods in Enzymology
Volume	510
ISSN (Print)	0076-6879
ISSN (Electronic)	1557-7988

Bibliographical note

Funding Information:
This research was supported by Grants-in-Aid for Scientific Research to K. I. (19688016 and 21688023), T. U. (21023010 and 21681017), and T. A. (20221006) from the Japanese Ministry of Education, Culture, Sports, and Technology; by a grant of the Knowledge Cluster Initiative to T. A.; by a Grant for Development of Technology for High Efficiency Bioenergy Conversion Project to M. S. (07003004-0) from the New Energy and Industrial Technology Development Organization; and by an Advanced Low Carbon Technology Research and Development Program from the Japan Science and Technology Agency to K. I. and T. U.

Copyright:
Copyright 2019 Elsevier B.V., All rights reserved.

Keywords

Biomass utilization
Cellulase
Cellulose
High-speed atomic force microscopy
Single-molecule observations
Trichoderma reesei

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10.1016/B978-0-12-415931-0.00009-4

Cite this

Igarashi, K., Uchihashi, T., Koivula, A., Wada, M., Kimura, S., Penttilä, M., Ando, T., & Samejima, M. (2012). Visualization of cellobiohydrolase i from trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy. In Methods in Enzymology (pp. 169-182). (Methods in Enzymology; Vol. 510). Academic Press Inc.. https://doi.org/10.1016/B978-0-12-415931-0.00009-4

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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.",

keywords = "Biomass utilization, Cellulase, Cellulose, High-speed atomic force microscopy, Single-molecule observations, Trichoderma reesei",

author = "Kiyohiko Igarashi and Takayuki Uchihashi and Anu Koivula and Masahisa Wada and Satoshi Kimura and Merja Penttil{\"a} and Toshio Ando and Masahiro Samejima",

note = "Funding Information: This research was supported by Grants-in-Aid for Scientific Research to K. I. (19688016 and 21688023), T. U. (21023010 and 21681017), and T. A. (20221006) from the Japanese Ministry of Education, Culture, Sports, and Technology; by a grant of the Knowledge Cluster Initiative to T. A.; by a Grant for Development of Technology for High Efficiency Bioenergy Conversion Project to M. S. (07003004-0) from the New Energy and Industrial Technology Development Organization; and by an Advanced Low Carbon Technology Research and Development Program from the Japan Science and Technology Agency to K. I. and T. U. Copyright: Copyright 2019 Elsevier B.V., All rights reserved.",

year = "2012",

doi = "10.1016/B978-0-12-415931-0.00009-4",

language = "English",

series = "Methods in Enzymology",

publisher = "Academic Press Inc.",

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Igarashi, K, Uchihashi, T, Koivula, A, Wada, M, Kimura, S, Penttilä, M, Ando, T & Samejima, M 2012, Visualization of cellobiohydrolase i from trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy. in Methods in Enzymology. Methods in Enzymology, vol. 510, Academic Press Inc., pp. 169-182. https://doi.org/10.1016/B978-0-12-415931-0.00009-4

Visualization of cellobiohydrolase i from trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy. / Igarashi, Kiyohiko; Uchihashi, Takayuki; Koivula, Anu et al.
Methods in Enzymology. Academic Press Inc., 2012. p. 169-182 (Methods in Enzymology; Vol. 510).

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

TY - CHAP

T1 - Visualization of cellobiohydrolase i from trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy

AU - Igarashi, Kiyohiko

AU - Uchihashi, Takayuki

AU - Koivula, Anu

AU - Wada, Masahisa

AU - Kimura, Satoshi

AU - Penttilä, Merja

AU - Ando, Toshio

AU - Samejima, Masahiro

N1 - Funding Information: This research was supported by Grants-in-Aid for Scientific Research to K. I. (19688016 and 21688023), T. U. (21023010 and 21681017), and T. A. (20221006) from the Japanese Ministry of Education, Culture, Sports, and Technology; by a grant of the Knowledge Cluster Initiative to T. A.; by a Grant for Development of Technology for High Efficiency Bioenergy Conversion Project to M. S. (07003004-0) from the New Energy and Industrial Technology Development Organization; and by an Advanced Low Carbon Technology Research and Development Program from the Japan Science and Technology Agency to K. I. and T. U. Copyright: Copyright 2019 Elsevier B.V., All rights reserved.

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

KW - Biomass utilization

KW - Cellulase

KW - Cellulose

KW - High-speed atomic force microscopy

KW - Single-molecule observations

KW - Trichoderma reesei

UR - http://www.scopus.com/inward/record.url?scp=84861130110&partnerID=8YFLogxK

U2 - 10.1016/B978-0-12-415931-0.00009-4

DO - 10.1016/B978-0-12-415931-0.00009-4

M3 - Chapter

C2 - 22608726

AN - SCOPUS:84861130110

T3 - Methods in Enzymology

SP - 169

EP - 182

BT - Methods in Enzymology

PB - Academic Press Inc.

ER -

Visualization of cellobiohydrolase i from trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy

Abstract

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Bibliographical note

Keywords

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