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Title Single molecule study of cellulase hydrolysis of crystalline cellulose [electronic resource] : preprint / Y.-S. Liu ... [et al.].

Imprint Golden, CO : National Renewable Energy Laboratory, [2009]

Copies

Location Call No. OPAC Message Status
 Axe Federal Documents Online  E 9.17:NREL/CP-270-47301    ---  Available
Description 1 online resource ([11] p.) : ill. (some col.)
Series Conference paper ; NREL/CP-270-47301
Conference paper (National Renewable Energy Laboratory (U.S.)) ; NREL/CP-270-47301.
System Details Full text available via Internet in .pdf format. Adobe Acrobat Reader required.
Note Title from title screen (viewed January 12, 2010).
"December 2009."
"To be presented at the Society of Photo-Optical Instrumentation Engineers (SPIE) Photonics West 2010, San Francisco, California, 23-28 January 2010."
Bibliography Includes bibliographical references (p. 7-8).
Funding DE-AC36-08-GO28308.
BB072330
Summary Cellobiohydrolase-I (CBH I), a processive exoglucanase secreted by Trichoderma reesei, is one of the key enzyme components in a commercial cellulase mixture currently used for processing biomass to biofuels. CBH I contains a family 7 glycoside hydrolase catalytic module, a family 1 carbohydrate-binding module (CBM), and a highly-glycosylated linker peptide. It has been proposed that the CBH I cellulase initiates the hydrolysis from the reducing end of one cellulose chain and successively cleaves alternate -1,4-glycosidic bonds to release cellobiose as its principal end product. The role each module of CBH I plays in the processive hydrolysis of crystalline cellulose has yet to be convincingly elucidated. In this report, we use a single-molecule approach that combines optical (total internal reflection fluorescence microscopy or TIRF-M) and non-optical (atomic force microscopy or AFM) imaging techniques to analyze the molecular motion of CBM tagged with green fluorescence protein (GFP) and to investigate the surface structure of crystalline cellulose and changes made in the structure by CBM and CBH I. Preliminary results reveal a confined nanometer-scale movement of the TrCBM1-GFP bound to cellulose, decreases in cellulose crystal size, and increases in surface roughness during CBH I hydrolysis of crystalline cellulose.
Subject Cellulose 1,4-beta-cellobiosidase.
Atomic spectroscopy -- Congresses.
Total internal reflection (Optics) -- Congresses.
Atomic force microscopy -- Congresses.
Biomass chemicals.
Added Author Liu, Yousan.
SPIE (Society)
National Renewable Energy Laboratory (U.S.)
Gpo Item No. 0430-P-04 (online)
Sudoc No. E 9.17:NREL/CP-270-47301

 
    
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