Work

An Intracellular PHB Depolymerase from the Supernatant Fraction of Ralstonia eutropha H16 Cells

Year: 2007

Type: article

Abstract: 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.

Source: Kanagawa University Repository (Kanagawa University)

Authors: Tomoko Abe, 智子安部, Teruyuki Kobayashi, Terumi Saito, 光實齊藤

Language: English

Topic: biodegradable polymer synthesis and properties

Subfield: Biomaterials

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

OpenAlex ID: W15876369

FWCI:

Cites: 25

Cited by:

Related to: 10