Catabolism of 3-Nitrophenol by Ralstonia eutropha JMP 134
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چکیده
منابع مشابه
Repression of phenol catabolism by organic acids in Ralstonia eutropha.
During batch growth of Ralstonia eutropha (previously named Alcaligenes eutrophus) on phenol in the presence of acetate, acetate was found to be the preferred substrate; this organic acid was rapidly metabolized, and the specific rate of phenol consumption was considerably decreased, although phenol consumption was not abolished. This decrease corresponded to a drop in phenol hydroxylase and ca...
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Ralstonia eutropha H16 degraded (mobilized) previously accumulated poly(3-hydroxybutyrate) (PHB) in the absence of an exogenous carbon source and used the degradation products for growth and survival. Isolated native PHB granules of mobilized R. eutropha cells released 3-hydroxybutyrate (3HB) at a threefold higher rate than did control granules of nonmobilized bacteria. No 3HB was released by n...
متن کاملFormation of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) by PHA synthase from Ralstonia eutropha.
The acetoacetyl-CoA reductase and the polyhydroxyalkanoate (PHA) synthase from Ralstonia eutropha (formerly Alcaligenes eutrophus) were expressed in Escherichia coli, Klebsiella aerogenes, and PHA-negative mutants of R. eutropha and Pseudomonas putida. While expression in E. coli strains resulted in the accumulation of poly(3-hydroxybutyrate) [PHB], strains of R. eutropha, P. putida and K. aero...
متن کاملProduction of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from plant oil by engineered Ralstonia eutropha strains.
The polyhydroxyalkanoate (PHA) copolymer poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) [P(HB-co-HHx)] has been shown to have potential to serve as a commercial bioplastic. Synthesis of P(HB-co-HHx) from plant oil has been demonstrated with recombinant Ralstonia eutropha strains expressing heterologous PHA synthases capable of incorporating HB and HHx into the polymer. With these strains, howeve...
متن کاملFormate dehydrogenase from Ralstonia eutropha
1 Spectroscopic and kinetic properties of the molybdenum-containing, NAD+-dependent formate dehydrogenase from Ralstonia eutropha. Dimitri Niks, Jayant Duvvuru, Miguel Escalona, and Russ Hille Department of Biochemistry, University of California, Riverside, Riverside, CA 92521 Running title: Formate dehydrogenase from Ralstonia eutropha To whom correspondence should be addressed: Prof. Russ Hil...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1997
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.63.4.1421-1427.1997