TY - JOUR
T1 - A simple route for purifying extracellular poly(3-hydroxybutyrate)-depolymerase from penicillium pinophilum
AU - Panagiotidou, Elpiniki
AU - Konidaris, Constantinos
AU - Baklavaridis, Apostolos
AU - Zuburtikudis, Ioannis
AU - Achilias, Dimitris
AU - Mitlianga, Paraskevi
N1 - Publisher Copyright:
© 2014 Elpiniki Panagiotidou et al.
PY - 2014
Y1 - 2014
N2 - This work proposes the purification of an active and efficient enzyme, extracellular poly(3-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 poly(3-hydroxybutyrate) (PHB) films successfully, as it is demonstrated by the biodegradation test results provided here.
AB - This work proposes the purification of an active and efficient enzyme, extracellular poly(3-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 poly(3-hydroxybutyrate) (PHB) films successfully, as it is demonstrated by the biodegradation test results provided here.
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U2 - 10.1155/2014/159809
DO - 10.1155/2014/159809
M3 - Article
AN - SCOPUS:84911923469
SN - 2090-0406
VL - 2014
JO - Enzyme Research
JF - Enzyme Research
M1 - 159809
ER -