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: Contribution to journal › Article › Scientific › peer-review

16 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
Pages (from-to)	169-182
Journal	Methods in Enzymology
Volume	510
DOIs	https://doi.org/10.1016/B978-0-12-415931-0.00009-4
Publication status	Published - 22 May 2012
MoE publication type	A1 Journal article-refereed

Keywords

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

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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",

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

language = "English",

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pages = "169--182",

journal = "Methods in Enzymology",

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Visualization of cellobiohydrolase i from trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy. / Igarashi, Kiyohiko; Uchihashi, Takayuki; Koivula, Anu; Wada, Masahisa; Kimura, Satoshi; Penttilä, Merja; Ando, Toshio; Samejima, Masahiro.

In: Methods in Enzymology, Vol. 510, 22.05.2012, p. 169-182.

Research output: Contribution to journal › Article › Scientific › peer-review

TY - JOUR

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 - CA2: TK404 CA2: TK400 SDA: BIC ISI: BIOCHEMISTRY & MOLECULAR BIOLOGY

PY - 2012/5/22

Y1 - 2012/5/22

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

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JO - Methods in Enzymology

JF - Methods in Enzymology

SN - 0076-6879

ER -

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

Abstract

Keywords

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