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https://hdl.handle.net/2440/54953
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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 1572-8900 |
Statement of Responsibility: | 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 Purification Properties PHB hydrolysis Penicillium sp. |
DOI: | 10.1007/s10924-006-0031-6 |
Published version: | http://dx.doi.org/10.1007/s10924-006-0031-6 |
Appears in Collections: | Aurora harvest 5 Chemical Engineering publications |
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