Previous Article | Next Article ![]()
Appl Environ Microbiol. 1994 April; 60(4): 1347-1352
Copyright © 1994, American Society for Microbiology. All Rights Reserved.

Department of Microbiology, Wageningen Agricultural University, 6703 CT Wageningen, The Netherlands
ABSTRACT
Bacteroides xylanolyticus X5-1 was grown in pure culture and in mixed culture with Methanospirillum hungatei JF-1 under xylose limitation in the chemostat. In the pure culture, ethanol, acetate, CO2, and hydrogen were the products. In the mixed culture, acetate, CO2, and presumably hydrogen were the only products formed by B. xylanolyticus X5-1. The biomass yield of B. xylanolyticus X5-1 increased because of cocultivation. In cell extracts of the pure culture, both NAD- and NADP-dependent acetaldehyde dehydrogenase and ethanol dehydrogenase activities were found. In cell extracts of the mixed culture, activities of these enzymes were not detected. Inhibition of methanogenesis in the mixed culture by the addition of bromoethanosulfonic acid (BES) resulted in an accumulation of H2, ethanol, and formate. Immediately after the addition of BES, NAD-dependent acetaldehyde dehydrogenase and ethanol dehydrogenase activities were detected. After a short lag phase, a NADP-dependent ethanol dehydrogenase was also detectable. The induction of acetaldehyde dehydrogenase and ethanol dehydrogenase was inhibited by chloramphenicol, suggesting de novo synthesis of these enzymes. These results are consistent with a model in which the shift in product formation caused by interspecies electron transfer is regulated at the level of enzyme synthesis.
* Corresponding author. Mailing address: Department of Microbiology, Wageningen Agricultural University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands. Phone: +31-8370-83101. Fax: +31-8370-83829. Electronic mail address: fons.stams@algemeen.micr.wau.nl.
Present address: EAWAG, CH-8600 Dübendorf, Switzerland.
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»