In methanol-limited continuous cultures of the obligate methylotrophic bacterium Methylobacillus flagellatum grown at rates from 0.05 to 0.63 h-1, and also in an oxyturbidostat culture of M. flagellatum growing at the rate of 0.73 h-1, levels of methanol dehydrogenase, enzymes of formaldehyde oxidation (both linear and cyclic) and assimilation (RuMP cycle), a number of intermediary metabolism and TCA cycle enzymes and also 'dye-linked' formaldehyde dehydrogenase were determined. It was shown that the activities of dissimilatory enzymes, with the exception of 'dye-linked' formaldehyde dehydrogenase, decreased with increasing growth rate. Activities of assimilative enzymes and activities of the TCA cycle enzymes detected as well as the 'dye-linked' formaldehyde dehydrogenase activity, increased with increasing growth rate. A periplasmic location was shown for the latter enzyme and a role in formaldehyde detoxification was proposed.
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http://dx.doi.org/10.1007/BF00572699 | DOI Listing |
J Chromatogr B Analyt Technol Biomed Life Sci
January 2008
Process Biotechnology, University of Bayreuth, 95440 Bayreuth, Germany.
The objective of this study was to develop a method for the quantitative analysis of the methylamine concentration in fermentation broths of Hyphomicrobium zavarzinii ZV 580 cultures. For this purpose an established method for the quantification of free amino acids in such matrices was adapted and validated. The detection limit was 10 microM, the calibration curve showed good linearity (R2=0.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
December 2007
University of Bayreuth, 95440, Bayreuth, Germany.
The dye-linked formaldehyde dehydrogenase (dlFalDH) from Hyphomicrobium zavarzinii ZV 580 processes formaldehyde in a highly selective manner and without need for NAD(P). The enzyme thus has considerable potential for technical applications if the difficulties associated with its efficient production can be resolved. In this contribution, a fed-batch bioprocess is developed, which improves both the biomass production of H.
View Article and Find Full Text PDFArch Microbiol
December 2004
Institut für Molekulare Physiologie und Biotechnologie der Pflanzen, Universität Bonn, Kirschallee 1, 53115 Bonn, Germany.
faoA, the gene of the dye-linked NAD(P)-independent quinone-containing formaldehyde dehydrogenase of methylamine-grown Hyphomicrobium zavarzinii strain ZV 580 was sequenced and analyzed together with an apparent promoter region and adjoining genes in a 7.2-kb fragment of hyphomicrobial DNA. The formaldehyde dehydrogenase, identified as a periplasmic enzyme by its signal sequence, is distantly related to the soluble pyrroloquinoline-quinone-dependent glucose dehydrogenase of Acinetobacter calcoaceticus and to other predicted glucose dehydrogenase sequences.
View Article and Find Full Text PDFArch Microbiol
October 2002
Laboratoire de Biologie Moléculaire des Relations Plantes-Microorganismes, INRA/CNRS, BP27, 31326 Castanet-Tolosan, France.
Methylotrophic bacteria can grow on a number of substrates as energy source with only one carbon atom, such as methanol, methane, methylamine, and dichloromethane. These compounds are metabolized via the cytotoxin formaldehyde. The formaldehyde consumption pathways, especially the pathways for the oxidation of formaldehyde to CO(2) for energy metabolism, are a central and critical part of the metabolism of these aerobic bacteria.
View Article and Find Full Text PDFJ Bacteriol
December 2001
Department of Microbiology, Iowa State University, 205 Science Building, Ames, IA 50011, USA.
A membrane-associated, dye-linked formaldehyde dehydrogenase (DL-FalDH) was isolated from the obligate methylotroph Methylococcus capsulatus Bath. The enzyme was the major formaldehyde-oxidizing enzyme in cells cultured in high (above 1 micromol of Cu per mg of cell protein) copper medium and expressing the membrane-associated methane monooxygenase. Soluble NAD(P)(+)-linked formaldehyde oxidation was the major activity in cells cultured in low-copper medium and expressing the soluble methane monooxygenase (Tate and Dalton, Microbiology 145:159-167, 1999; Vorholt et al.
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