| Title : Purification and properties of poly(3-hydroxybutyrate) depolymerase from the fungus Paecilomyces lilacinus D218 - Oda_1997_Curr.Microbiol_34_230 |
| Author(s) : Oda Y , Osaka H , Urakami T , Tonomura K |
| Ref : Curr Microbiol , 34 :230 , 1997 |
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Abstract :
Poly(3-hydroxybutyrate) depolymerase was purified to homogeneity from the culture filtrate of Paecilomyces lilacinus D218 by column chromatography on CM-Toyopearl 650M and hydroxylapatite. The molecular weight of the enzyme was estimated to be 48,000 by SDS-PAGE. Maximal activity was observed near pH 7.0 and 45 degrees C. The Km and Vmax values for PHB were 0.13(mg/ml) and 3750 (U/mg protein), respectively. The enzyme hydrolyzed PHB and p-nitrophenyl fatty acids but not polycaprolactone and triglycerides. |
| PubMedSearch : Oda_1997_Curr.Microbiol_34_230 |
| PubMedID: 9058543 |
Oda Y, Osaka H, Urakami T, Tonomura K (1997)
Purification and properties of poly(3-hydroxybutyrate) depolymerase from the fungus Paecilomyces lilacinus D218
Curr Microbiol
34 :230
Oda Y, Osaka H, Urakami T, Tonomura K (1997)
Curr Microbiol
34 :230