Title: Purification and properties of poly(3-hydroxybutyrate) depolymerase from the fungus Paecilomyces lilacinus D218 Oda Y, Osaka H, Urakami T, Tonomura K Ref: Curr Microbiol, 34:230, 1997 : PubMed
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.
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Oda Y, Osaka H, Urakami T, Tonomura K (1997) Purification and properties of poly(3-hydroxybutyrate) depolymerase from the fungus Paecilomyces lilacinus D218 Curr Microbiol34: 230-2
Oda Y, Osaka H, Urakami T, Tonomura K (1997) Curr Microbiol34: 230-2
