@article{oai:kanagawa-u.repo.nii.ac.jp:00006938,
 author = {Abe, Tomoko and 安部, 智子 and Kobayashi, Teruyuki and 小林, 照幸 and Saito, Terumi and 齊藤, 光實},
 journal = {Science Journal of Kanagawa University},
 month = {May},
 note = {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.},
 pages = {11--17},
 title = {An Intracellular PHB Depolymerase from the Supernatant Fraction of Ralstonia eutropha H16 Cells},
 volume = {18},
 year = {2007}
}