Preliminary Program subject to change
15C18 Advances in Extreme Biocatalysis
OverviewBiological production of complex molecules has many advantages over chemical synthesis methods including much higher reaction specificity, few or no side reactions, production of a single chiral form, etc. However, under many desirable industrial process conditions (high or low temperatures or pH, high salt concentration, high pressure, etc.), traditional biological methods quickly and irreversibly lose activity. This session would focus on progress being made in development of industrially relevant biological processing under extreme conditions. Papers would be sought that cover the entire range of development from discovery of novel enzymes and pathways in extreme organisms to industrial production using these organisms and enzymes. Examples would include characterization of relevant pathways and enzymes from extreme organisms, advances in methods to express active extreme enzymes in mesophilic hosts, overcoming issues related to scale up of bench scale processes, and industrial scale production. The potential audience would be individuals from academia, government labs, and industry involved in this type of work.
Primary SponsorBioengineering (15c)

Chair

Vicki S. Thompson
Staff Engineer
Biotechnology Department
Idaho National Engineering and Environmental Laboratory
P.O. Box 1625
Idaho Falls, ID 83415-2203
Phone Number: (208) 526-8833
Fax Number: (208) 526-0828
Email: THOMVS@inel.gov

CoChair

Jennifer Baeseman
NSF Microbial Biology Postdoctoral Research Fellow
Department of Geosciences
Princeton University
M45 Guyot Hall
Princeton, NJ 08544-1003
Phone Number: 609-258-6294
Fax Number: 609-258-0796
Email: baeseman@princeton.edu
Bioconversion of Biomass Using a Coculture of Thermotoga Maritima and Methanococcus Jannaschii
T. Akim Nilausen, Chemical and Biochemical Engineering, University of Iowa, 4133 Seamans Center, Iowa City, IA 52242 and Tonya L. Peeples, Chemical and Biochemical Engineering, University of Iowa, 4128 Seamans Center, Iowa City, IA 52242
Thermoacidophilic Cellulases and Hemicellulases from Alicyclobacillus Acidocaldarius
Vicki S. Thompson1, David N. Thompson2, Kastli D. Schaller3 and William A. Apel3, (1)Biotechnology Department, Idaho National Laboratory, P.O. Box 1625, Idaho Falls, ID 83415-2203, (2)Idaho National Laboratory, Biological Sciences Department, P.O. Box 1625, Idaho Falls, ID 83415-2203, (3)Biological Sciences, Idaho National Laboratory, P.O. Box 1625, Idaho Falls, ID 83415-2203
Complex Hyperthermophilic Proteases: the Effect of Beta Protein Content on Biochemical and Biophysical Properties of Proteasomes
Joshua K. Michel, Lara S. Madding, Keith R. Shockley, Shannon B. Conners, Kevin L. Epting, Matthew R. Johnson, Sabrina Tachdjian and Robert M. Kelly, Chemical Engineering, North Carolina State University, NCSU Box 7270, Raleigh, NC 27695
Effects of Mass-Transfer and Kinetic Parameters on Biocatalytic Activity of Immobilized Burkholderia Cepacia Lipase in a Packed-Bed Reactor
Hemachand Jaladi, University of Cincinnati, 420,Riddle Road, #2A, Cincinnati, OH 45220, Amit Katiyar, University of Cincinnati, P.O. Box 210012, Cincinnati, OH 45221-0012, Vadim V. Guliants, Department of Chemical and Materials Engineering, University of Cincinnati, Cincinnati, OH 45221-0012 and Neville G. Pinto, Chemical & Materials Engineering, University of Cincinnati, P.O. Box 210012, Cincinnati, OH 45221-0012
Break
Regulation of Carbon Monoxide Dehydrogenase Gene Complexes by Cooa in Carboxydothermus Hydrogenoformans
Deborah T. Newby1, Stephen Techtmann2, Joni M. Barnes1, Heather G. Silverman1, Jeffrey A. Lacey1, Kevin Epting1, Albert S. Colman2, Dennis L. Maeder2 and Frank T. Robb2, (1)Biological Sciences, Idaho National Laboratory, 1765 North Yellowstone Highway, Idaho Falls, ID 83415, (2)University of Maryland, Center of Marine Biotechnology, Columbus Center, Suite 236, 701 East Pratt Street, Baltimore, MD 21202
Proteomic Analysis of a Hydrogen Producing Thermophile Carboxydothermus Hydrogenoformans
Vicki S. Thompson, Kevin Epting, Kastli D. Schaller and David W. Reed, Biological Sciences, Idaho National Laboratory, P.O. Box 1625, Idaho Falls, ID 83415-2203

Food, Pharmaceutical & Bioengineering Division