Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

The hemicellulases from the ethanologenic thermophile: Themoanaerobacter ethanolius

Technical Report ·
DOI:https://doi.org/10.2172/5012379· OSTI ID:5012379
Previously, we had only obtained extremely low xylanase activity in cultures of {ital Thermoanaerobacter ethanolicus} strain JW200, despite demonstrated xylan hydrolysis. We were not able to increase the enzyme activity or concentrate it in solution. Therefore, we decided to isolate new strains of thermophilic anaerobes with higher xylanase activity as a future source for cloning xylanases into {ital T. ethanolicus}. We now have organisms exhibiting 100-fold higher xylanase activity than JW200, but still cannot isolate or concentrate the enzyme activity except at very low yields. We have concentrated and partially purified a xylanase from strain N.D. using preparative matrix-free isoelectric focusing. We have also purified to homogeneity and partially characterized a xylosidase from {ital T. ethanolicus}. We have detected and measured arabinosidase and acetyl esterase activity in {ital T.ethanolicus}, {ital Clostridium thermohydrosulfuricum} and strain N.D. 7 refs., 2 tabs. (MHB)
Research Organization:
Georgia Univ., Athens, GA (United States). Research Foundation
Sponsoring Organization:
DOE; USDOE, Washington, DC (United States)
DOE Contract Number:
FG09-89ER14059
OSTI ID:
5012379
Report Number(s):
DOE/ER/14059-1; ON: DE92001859
Country of Publication:
United States
Language:
English