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Polymer-Plastics Technology and Engineering Volume 48, 2008 - Issue 1
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Original Articles

Purification and Characterization of Extracellular Poly(β-hydroxybutyrate) Depolymerase from Penicillium sp. DS9701-D2

Hailu Zhou School of Life Sciences, Northeast Normal University, Changchun, China
,
Zhanyong Wang School of Life Sciences, Northeast Normal University, Changchun, China; School of Environmental and Biological Engineering, Liaoning Shihua University, Fushun, China
,
Shan Chen School of Life Sciences, Northeast Normal University, Changchun, ChinaCorrespondence[email protected]
,
Dongbo Liu School of Life Sciences, Northeast Normal University, Changchun, China
&
Hongmei Xia School of Life Sciences, Northeast Normal University, Changchun, China
Pages 58-63 | Published online: 17 Dec 2008
 
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Abstract

An extracellular poly (β-hydroxybutyrate) (PHB) depolymerase was purified from Penicillium sp. DS9701-D2. The molecular weight of the enzyme was estimated to be about 46.8 KDa by sodium dodecyl sulfate—polyacrylamide gel electrophoresis. The isoelectric point of 7.6 for the enzyme was determined by capillary electrophoresis. The optimum enzyme activity was detected at 30°C and pH 5.0. It was found that Na+ and K+ enhance the enzyme activity, whereas Zn2+, Mg2+, Cu2+, and Fe2+ inhibit it. The secondary structure of the enzyme was measured by circular dichroism (CD) spectroscopy. The main degradation product of depolymerase was indentified as 3-hydroxybutyrate dimer by mass spectrometer (MS) analysis.

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Related Research Data

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