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https://hdl.handle.net/2440/54953
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dc.contributor.author | Liu, H. | - |
dc.contributor.author | Zhang, H. | - |
dc.contributor.author | Chen, S. | - |
dc.contributor.author | Liu, D. | - |
dc.contributor.author | Xia, H. | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Journal of Polymers and the Environment, 2006; 14(4):419-426 | - |
dc.identifier.issn | 1566-2543 | - |
dc.identifier.issn | 1572-8900 | - |
dc.identifier.uri | http://hdl.handle.net/2440/54953 | - |
dc.description.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. | - |
dc.description.statementofresponsibility | Hongyu Liu, Hu Zhang, Shan Chen, Dongbo Liu and Hongmei Xia | - |
dc.language.iso | en | - |
dc.publisher | Springer New York LLC | - |
dc.source.uri | http://dx.doi.org/10.1007/s10924-006-0031-6 | - |
dc.subject | PHB depolymerase | - |
dc.subject | Purification | - |
dc.subject | Properties | - |
dc.subject | PHB hydrolysis | - |
dc.subject | Penicillium sp. | - |
dc.title | Purification and properties of a poly (β-hydroxybutyrate) depolymerase from penicillium sp. | - |
dc.title.alternative | Purification and properties of a poly (beta-hydroxybutyrate) depolymerase from penicillium sp. | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1007/s10924-006-0031-6 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Zhang, H. [0000-0003-4178-6401] | - |
Appears in Collections: | Aurora harvest 5 Chemical Engineering publications |
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