نتایج جستجو برای: ralstonia eutropha h16

تعداد نتایج: 2604  

Journal: :Journal of bacteriology 2010
Christopher J Brigham Charles F Budde Jason W Holder Qiandong Zeng Alison E Mahan Chokyun Rha Anthony J Sinskey

Ralstonia eutropha H16 is capable of growth and polyhydroxyalkanoate production on plant oils and fatty acids. However, little is known about the triacylglycerol and fatty acid degradation pathways of this bacterium. We compare whole-cell gene expression levels of R. eutropha H16 during growth and polyhydroxyalkanoate production on trioleate and fructose. Trioleate is a triacylglycerol that ser...

Journal: :Physical chemistry chemical physics : PCCP 2011
Yvonne Rippers Tillmann Utesch Peter Hildebrandt Ingo Zebger Maria Andrea Mroginski

Structural models for the Ni-B state of the wild-type and C81S protein variant of the membrane-bound [NiFe] hydrogenase from Ralstonia eutropha H16 were derived by applying the homology model technique combined with molecular simulations and a hybrid quantum mechanical/molecular mechanical approach. The active site structure was assessed by comparing calculated and experimental IR spectra, conf...

Journal: :Microbiology 2007
Sonja Weinitschke Karin Denger Alasdair M Cook Theo H M Smits

The degradation of taurine, isethionate and sulfoacetate in Cupriavidus necator (Ralstonia eutropha) H16 was shown by enzyme assays to be inducible, and each pathway involved sulfoacetaldehyde, which was subject to phosphatolysis by a common sulfoacetaldehyde acetyltransferase (Xsc, H16_B1870) to yield acetyl phosphate and sulfite. The neighbouring genes encoded phosphate acetyltransferase (Pta...

2016
Bat-Erdene Jugder Helene Lebhar Kondo-Francois Aguey-Zinsou Christopher P. Marquis

The soluble hydrogenase (SH) from Ralstonia eutropha H16 is a promising candidate enzyme for H2-based biofuel application as it favours H2 oxidation and is relatively oxygen-tolerant. In this report, bioprocess development studies undertaken to produce and purify an active SH are described, based on the methods previously reported [1], [2], [3], [4]. Our modifications are: •Upstream method opti...

Journal: :Applied and environmental microbiology 2008
Keiichi Uchino Terumi Saito Dieter Jendrossek

The recently finished genome sequence of Ralstonia eutropha H16 harbors nine genes that are thought to encode functions for intracellular depolymerization (mobilization) of storage poly(3-hydroxybutyrate) (PHB). Based on amino acid similarities, the gene products belong to four classes (PhaZa1 to PhaZa5, PhaZb, PhaZc, and PhaZd1/PhaZd2). However, convincing direct evidence for the in vivo roles...

Journal: :Journal of Molecular Microbiology and Biotechnology 2009

2015
Janice S. Chen Brendan Colón Brendon Dusel Marika Ziesack Jeffrey C. Way Joseph P. Torella Guo-Qiang Chen

Ralstonia eutropha H16 is a facultatively autotrophic hydrogen-oxidizing bacterium capable of producing polyhydroxybutyrate (PHB)-based bioplastics. As PHB's physical properties may be improved by incorporation of medium-chain-length fatty acids (MCFAs), and MCFAs are valuable on their own as fuel and chemical intermediates, we engineered R. eutropha for MCFA production. Expression of UcFatB2, ...

2011
Franziska Hempel Andrew S Bozarth Nicole Lindenkamp Andreas Klingl Stefan Zauner Uwe Linne Alexander Steinbüchel Uwe G Maier

BACKGROUND Poly-3-hydroxybutyrate (PHB) is a polyester with thermoplastic properties that is naturally occurring and produced by such bacteria as Ralstonia eutropha H16 and Bacillus megaterium. In contrast to currently utilized plastics and most synthetic polymers, PHB is biodegradable, and its production is not dependent on fossil resources making this bioplastic interesting for various indust...

Journal: :Biochemical Society transactions 2005
A Büsch K Strube B Friedrich R Cramm

Nitric oxide reduction in Ralstonia eutropha H16 is catalysed by the quinol-dependent NO reductase NorB. norB and the adjacent norA form an operon that is controlled by the sigma(54)-dependent transcriptional activator NorR in response to NO. A NorR derivative containing MalE in place of the N-terminal domain binds to a 73 bp region upstream of norA that includes three copies of the putative up...

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