Back to Results
First PageMeta Content
Transferases / Proteins / Glycogen phosphorylase / Enzymes / Intein / Phosphorylase / Clostridium thermocellum / Dextrin / RNA / Chemistry / Biology / Catalysis


Thermophilic α-glucan phosphorylase from Clostridium thermocellum: Cloning, characterization and enhanced thermostability
Add to Reading List

Document Date: 2012-08-03 09:41:25


Open Document

File Size: 937,57 KB

Share Result on Facebook

City

Blacksburg / Bradford / Philadelphia / Louis / St. Louis / /

Company

FMC / AMP / T.B. Eronina N.A. / Millipore / Elsevier B.V. / GP / Oak Ridge National Laboratory / Bio-Rad / /

Country

United States / /

/

Facility

Oak Ridge National Laboratory / A Seitz Hall / USA Institute / Virginia Polytechnic Institute / State University / /

/

IndustryTerm

catalytic machinery / metal ions / potential applications / ve glucose unit binding site / industrial applications / catalytic site / chemicals / web version / /

Organization

Bioprocessing and Biodesign Center / USA Institute for Critical Technology and Applied Science / USDA / BioEnergy Science Center / Dupont Young Faculty / Biological Systems Engineering Department / DOE Bioenergy Science Center / Polytechnic Institute / State University / /

Person

W. Miller / Nat / S.G. Bazhina / V / Joe Rollin / G.K. Schulte / Heng Percival Zhang / Fisher Scienti / Gene Struct / Jonathan Mielenz / T. Bernard / V / /

/

Position

Corresponding author / Air Force Young Investigator / cellulose specialist / Fisher / D.J. / /

ProvinceOrState

Virginia / Tennessee / /

PublishedMedium

PLoS ONE / /

Technology

protein engineering / biotransformations / hybridization / Biotechnology / polymerization / Cloning / directed evolution / biofuels / gene expression / DNA sequencing / Biocatalysis / Bioprocessing / Dialysis / /

URL

www.elsevier.com/locate/molcatb / http /

SocialTag