PURIFICATION AND PROPERTIES OF POLY(3-HYDROXYBUTYRATE) DEPOLYMERASE FROM THE FUNGUS PAECILOMYCES-LILACINUS D218

Authors
ODA Y OSAKA H URAKAMI T TONOMURA K
Citation
Y. Oda et al., PURIFICATION AND PROPERTIES OF POLY(3-HYDROXYBUTYRATE) DEPOLYMERASE FROM THE FUNGUS PAECILOMYCES-LILACINUS D218, Current microbiology, 34(4), 1997, pp. 230-232
Citations number
13
Categorie Soggetti
Microbiology
Journal title
Current microbiology → ACNP
ISSN journal
03438651
Volume
34
Issue
4
Year of publication
1997
Pages
230 - 232
Database
ISI
SICI code
0343-8651(1997)34:4<230:PAPOPD>2.0.ZU;2-S
Abstract
Poly(3-hydroxybutyrate) depolymerase was purified to homogeneity from the culture filtrate of Paecilomyces lilacinus D218 by column chromato graphy 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 ans 45 degrees C. The K-m and V-max walues f or PHB were 0.13 (mg/ml) and 3750 (U/mg protein), respectively. The en zyme hydrolyzed PHB and p-nitrophenyl fatty acids but not polycaprolac tone and triglycerides.