Biochemical and molecular characterization of the polyhydroxybutyrate depolymerase of Comamonas acidovorans YM1609, isolated from freshwater

A research was conducted to study the purification of the extracellular polyhydroxybutyrate (PHB) depolymerase from the culture supernatant of Comamonas acidovorans and to examine its biochemical and kinetic properties. The function of the putative substrate-binding domain was determined through a fusion protein with glutathione S-transferase formed in Escherichia coli. Results indicated that the PHB depolymerase was composed of discrete domains connected by a linker region.