ISSN:
1572-8900
Keywords:
Poly(3-hydroxybutyrate)
;
poly(3-hydroxybutyrate) depolymerase
;
extracellular enzyme
;
N-terminal amino acid sequence
;
enzyme purification
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
,
Energy, Environment Protection, Nuclear Power Engineering
,
Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
Notes:
Abstract Five extracellular PHB depolymerases of bacteria isolated from various sources were purified to electrophoretic homogeneity and compared with known extracellular PHB depolymerase fromAlcaligenes faecalis T1. The molecular mass of these enzymes were all around 40–50 kDa. Nonionic detergent, diisopropylfluorophosphate and dithiothreitol inhibited the PHB depolymerase activity of all these enzymes. Trypsin abolished PHB depolymerase activity, but not theD-3-hydroxybutyric acid dimer hydrolase activity of all the enzymes. These results showed that the basic properties of these PHB depolymerases resemble those of theA. faecalis T1 enzyme. Analysis ofN-terminal amino acid sequence of the purified enzymes revealed that these enzymes includingA. faecalis T1 enzyme fall into three groups.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02067789
