Wang_2012_World.J.Microbiol.Biotechnol_28_2395

Reference

Title : Purification and characterization of an extracellular poly(3-hydroxybutyrate-co-3-hydroxyvalerate) depolymerase from Acidovorax sp. HB01 - Wang_2012_World.J.Microbiol.Biotechnol_28_2395
Author(s) : Wang Z , Gao J , Li L , Jiang H
Ref : World J Microbiol Biotechnol , 28 :2395 , 2012
Abstract :

The poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV)-degrading strain Acidovorax sp. HB01 was isolated from an activated sludge sample. A novel PHBV depolymerase with a molecular weight of 43.4 kDa was purified to homogeneity from the culture supernatant of the HB01 strain. The optimum pH and temperature of the PHBV depolymerase were 7.0 and 50 degreesC, respectively. The PHBV depolymerase can also degrade polyhydroxybutyrate, poly (3-hydroxybutyrate-co-4-hydroxybutyrate), and poly(caprolactone); however, the PHBV degradation activity of the depolymerase is higher than its activity against the other polymers. Effect of metal ions and various inhibitors on the PHBV depolymerase activity was examined. The addition of Na(+), K(+), and Ca(2+) markedly increased the hydrolysis rate, whereas the enzyme activity was inhibited by Zn(2+), Mg(2+), Mn(2+), and particularly by Cu(2+) and Fe(2+). Ethylenediaminetetraacetic acid was found to have a significant inhibitory effect. The main degradation product of depolymerase was identified as the 3-hydroxybutyric acid monomer and 3-hydroxyvaleric acid monomers via mass spectrometry.

PubMedSearch : Wang_2012_World.J.Microbiol.Biotechnol_28_2395
PubMedID: 22806113

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Citations formats

Wang Z, Gao J, Li L, Jiang H (2012)
Purification and characterization of an extracellular poly(3-hydroxybutyrate-co-3-hydroxyvalerate) depolymerase from Acidovorax sp. HB01
World J Microbiol Biotechnol 28 :2395

Wang Z, Gao J, Li L, Jiang H (2012)
World J Microbiol Biotechnol 28 :2395