Hemicellulases from the ethanologenic thermophile Thermoanaerobacter ethanolicus and related anaerobic thermophiles. Final report, September 1992--June 1996

Technical Report · Fri May 01 04:00:00 EDT 1998

DOI:https://doi.org/10.2172/604352· OSTI ID:604352

Wiegel, J

The SHORT TERM GOALS of this application were to characterize hemicellulases from anaerobic thermophiles on the biochemical and molecular level to extend the presently limited knowledge of hemicellulases in anaerobic thermophilic bacteria. This objective includes the following TASKS: (1) Traditional purification and biochemical/biophysical characterization of xylanases from the newly isolated, slightly alkalitolerant strain NDF190, and the slightly acid-tolerant strain YS485, both with high xylanolytic activities, and of the 4-0-methyl glucuronidase and arabinosidase from strain NDF190 and the acetyl (xylan) esterase from T. ethanolicus. This also includes determining the N-terminal sequences and obtaining gene probes. (2) Elucidation of the regulation of hemicellulolytic enzymes in anaerobic thermophiles. (3) To clone into E. coli and identify the multiplicity of the enzymes involved in hemicellulose degradation by T. ethanolicus and other suitable organisms. (4) To purify and characterize the recombinant enzymes with the goal of identifying the best enzymes for cloning into the ethanologenic T. ethanolicus to obtain an optimized hemicellulose utilization by this bacterium (one of our long term goals).

• Research Organization: Georgia Univ., Athens, GA (United States)
• Sponsoring Organization: USDOE Office of Energy Research, Washington, DC (United States)
• DOE Contract Number: FG09-89ER14059
• OSTI ID: 604352
• Report Number(s): DOE/ER/14059--T2; ON: DE98005007
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
BACTERIA
BIODEGRADATION
CLONING
ENZYME ACTIVITY
ESCHERICHIA COLI
GLUCURONIDASE
HEMICELLULOSE
METABOLISM
PROBES
PROGRESS REPORT