A Simple Route for Purifying Extracellular Poly3-hydroxybutyrate-depolymerase from Penicillium pinophilumReportar como inadecuado




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Enzyme Research - Volume 2014 2014, Article ID 159809, 6 pages -

Research Article

Department of Mechanical and Industrial Design Engineering, TEI of Western Macedonia, 50100 Kozani, Greece

Department of Chemistry, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece

Laboratory of Biotechnology, Department of Biological Applications and Technologies, University of Ioannina, 45100 Ioannina, Greece

Laboratory of Biochemistry, Department of Biological Applications and Technologies, University of Ioannina, 45100 Ioannina, Greece

Department of Chemical and Petroleum Engineering, United Arab Emirates University, Al Ain, UAE

Depertment of Agricultural Technology, School of Agriculture Technology, Food Technology and Nutrition, TEI of Western Macedonia, Terma Kontopoulou, 53100 Florina, Greece

Received 10 July 2014; Revised 10 September 2014; Accepted 10 September 2014; Published 23 September 2014

Academic Editor: Denise Freire

Copyright © 2014 Elpiniki Panagiotidou et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

This work proposes the purification of an active and efficient enzyme, extracellular poly3-hydroxybutyrate PHB-depolymerase, suitable for industrial applications. This is achieved by the application of an easy, fast, and cheap route, skipping the chromatography step. Chromatography with one or two columns is a common step in the purification procedure, which however renders the isolation of the enzyme a time consuming and an expensive process. A strain of the fungus Penicillium pinophilum ATCC 9644 is used for the isolation of extracellular PHB-depolymerase. The molecular weight of the purified enzyme is about 35 kDa and is estimated by gel electrophoresis SDS-PAGE, 12% polyacrylamide. The enzymatic activity of the isolated enzyme is determined to be 3.56-fold similar to that found by other researchers that have used chromatography for the isolation. The as-isolated enzyme disintegrates the poly3-hydroxybutyrate PHB films successfully, as it is demonstrated by the biodegradation test results provided here.





Autor: Elpiniki Panagiotidou, Constantinos Konidaris, Apostolos Baklavaridis, Ioannis Zuburtikudis, Dimitris Achilias, and Paraskevi

Fuente: https://www.hindawi.com/



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