Single molecule study of cellulase hydrolysis of crystalline cellulose : preprint / Y.-S. Liu [and others].

Format:

Book

Government document

Contributor:

Liu, Yousan

SPIE (Society)

National Renewable Energy Laboratory (U.S.)

Series:

Conference paper (National Renewable Energy Laboratory (U.S.)) ; NREL/CP-270-47301.

Conference paper ; NREL/CP-270-47301

Language:

English

Subjects (All):

Cellulose 1,4-beta-cellobiosidase.

Atomic spectroscopy--Congresses.

Atomic spectroscopy.

Total internal reflection (Optics)--Congresses.

Total internal reflection (Optics).

Atomic force microscopy--Congresses.

Atomic force microscopy.

Biomass chemicals.

Genre:

Congresses.

technical reports.

proceedings (reports)

Technical reports

Conference papers and proceedings

Technical reports.

Conference papers and proceedings.

Physical Description:

1 online resource ([11] pages) : illustrations (some color)

Place of Publication:

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

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 ß-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.

Notes:

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."

Includes bibliographical references (pages 7-8).

OCLC:

497074471