An Intracellular PHB Depolymerase from the Supernatant Fraction of Ralstonia eutropha H16 Cells
スポンサーリンク
概要
- 論文の詳細を見る
A poly (3-hydroxybutyrate) (PHB) depolymerase was purified 4, 400-fold from the supernatant fraction of Ralstonia eutropha cells through fractionation with ammonium sulfate and chromatography with Toyopearl DEAE, Q Sepharose, and Toyopearl Ether. The partially purified preparation showed a high level of specific activity to hydrolyze amorphous PHB, comparable to PhaZd from R. eutropha. The degradation was inhibited by diisopropylphosphate (10mM) and dithiothreitol (100mM). Most of the degradation products were 3-hydroxybutyrate oligomers. The properties of the enzyme closely resembled those of PhaZd, but some differences were observed. This distinction from PhaZd was discussed.
- 神奈川大学の論文
- 2007-05-25
著者
-
Kobayashi Teruyuki
Laboratory Of Molecular Microbiology Department Of Biological Sciences Faculty Of Science Kanagawa U
-
Saito Terumi
Laboratory Of Molecular Microbiology Department Of Biological Sciences Faculty Of Science Kanagawa U
-
Saito Terumi
Laboratory Of Molecular Microbiology Department Of Biological Science Faculty Of Science Kanagawa Un
-
Abe Tomoko
Laboratory of Molecular Microbiology, Department of Biological Sciences, Faculty of Science, Kanagaw
-
Abe Tomoko
Laboratory Of Molecular Microbiology Department Of Biological Sciences Faculty Of Science Kanagawa U
-
Kobayashi Teruyuki
Laboratory Of Molecular Microbiology Department Of Biological Sciences Faculty Of Science Kanagawa U
関連論文
- An Intracellular PHB Depolymerase from the Supernatant Fraction of Ralstonia eutropha H16 Cells
- Characterization of Two 3-Hydroxybutyrate Dehydrogenases in Poly(3-Hydroxybutyrate)-Degradable Bacterium, Ralstonia pickettii T1 (MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)
- Characterization of Third 3-Hydroxybutyrate Dehydrogenase in Ralstonia pickettii T1
- Biochemical and Genetic Characterization of a D(-)-3-Hydroxybutyrate Dehydrogenase from Acidovorax sp. Strain SA1
- Catalytic Triad of Intracellular Poly(3-Hydroxybutyrate) Depolymerase(PhaZ1) in Ralstonia eutropha H16
- Fermentative Production of (R)-(-)-3-Hydroxybutyrate Using 3-Hydroxybutyrate Dehydrogenase Null Mutant of Ralstonia eutropha and Recombinant Escherichia coli(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)
- Cloning and Sequencing of the Poly (3-hydroxybutyrate)(PHB) Synthase Gene from Purple Non-Sulfur Bacteria Rhodospirillum centenum and Expression of the Gene in Escherichia coli
- Purification and Molecular Cloning of an Intracellular 3-Hydroxybutyrate-Oligomer Hydrolase from Paucimonas lemoignei(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Cloning of an Intracellular D(-)-3-Hydroxybutyrate-Oligomer Hydrolase Gene from Ralstonia eutropha H16 and Identification of the Active Site Serine Residue by Site-Directed Mutagenesis
- Thiolysis of Poly(3-hydroxybutyrate) with Polyhydroxyalkanoate Synthase from Ralstonia eutropha