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Clostridium thermocellum / Cellulase / Hydrolysis / Enzyme / Cellulosome / Catalysis / Clostridium / Carbohydrate-binding module / Glycoside hydrolase family 48 / Chemistry / Cellulose / Clostridiaceae


AEM Accepts, published online ahead of print on 15 July 2011 Appl. Environ. Microbiol. doi:[removed]AEM[removed]Copyright © 2011, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Rese
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Document Date: 2011-08-09 16:39:26


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Oak Ridge National Laboratory / D. G. S. A. / Agilent 55 Technologies / Spiridonov N. A. / Sigma-Aldrich / Proc Natl Acad Sci U S A / Bio-Rad / /

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pence / /

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Facility

Cornell University / Biotechnology Building / /

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active site / transportation fuels / catalytic site / high activation energy / product binding site / energy system / cellulose chain / soluble products / /

Organization

U.S. Department of Energy / Department of Molecular Biology and Genetics / American Society for Microbiology / BioEnergy Science Center / office of Biological and Environmental Research / office of Science / Cornell University / /

Person

H. David Wu / R. A. Warren / Wen / D. Zhang / V / R. C. Miller / Jr. / David B. Wilson / /

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Position

author / /

Product

G6 / SC / Nokia E55 Smartphone / sodium acetate / /

ProvinceOrState

South Carolina / /

PublishedMedium

PLoS One / Environmental Research / Molecular Biology / /

Technology

Protein engineering / Proteomics / biofuels / Biotechnology / directed mutagenesis / Cloning / /

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