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Type: Journal article
Title: Purification and properties of a poly (β-hydroxybutyrate) depolymerase from penicillium sp.
Other Titles: Purification and properties of a poly (beta-hydroxybutyrate) depolymerase from penicillium sp.
Author: Liu, H.
Zhang, H.
Chen, S.
Liu, D.
Xia, H.
Citation: Journal of Polymers and the Environment, 2006; 14(4):419-426
Publisher: Springer New York LLC
Issue Date: 2006
ISSN: 1566-2543
Statement of
Hongyu Liu, Hu Zhang, Shan Chen, Dongbo Liu and Hongmei Xia
Abstract: An extracellular poly (β-hydroxybutyrate) (PHB) depolymerase was purified from a Penicillium sp. DS9701-09a by centrifugation, ultrafiltration, precipitation and gel filtration chromatography. The specific activity of the purified enzyme was 37.9-folds higher than that of the culture supernatant and the recovery yield was 11.8%. The PHB deploymerase molecular mass was 44.8 kDa from analysis of both Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Matrix-assisted laser desorption-time-of-flight (MALDI-TOF) mass spectrometer. The isoelectric point of 6.7 for the enzyme was determined by a two-dimensional electrophoresis. The optimum enzyme activity was observed at a temperature of 50 °C and pH 5.0. The apparent K m of the enzyme was found to be 1.35 mg/mL. The PHB depolymerase consisted of 16 kinds of normal amino acids. The secondary structure of the enzyme was determined by CD spectrum. α-helix and β-turn were found to be 66% and 34% for the enzyme without ammonium sulphite. Chemical inhibition on the PHB depolymerase activity was examined and EDTA was found to have a significantly inhibitory effect.
Keywords: PHB depolymerase
PHB hydrolysis
Penicillium sp.
DOI: 10.1007/s10924-006-0031-6
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Chemical Engineering publications

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