Polycaprolactone depolymerase produced by the bacterium Alcaligenes faecalis.
Several microorganisms were isolated as bacteria degrading polycaprolactone (PCL), and one of them, a strain B273 identified as Alcaligenes faecalis, was selected. Because this strain produced only slight PCL depolymerase activity, the hyperproducing mutant, TS22, was isolated after UV irradiation. Synthesis of PCL depolymerase was derepressed, probably based on the altered regulation of metabolic pathways in strain TS22. The partially purified enzyme hydrolyzed p-nitrophenyl fatty acids and triglycerides other than PCL, but not poly(3-hydroxybutyrate), indicating that PCL depolymerase may be a kind of lipase.
Oda
Y
Y
Department of Food Science and technology, Fukuyama University, Japan. oda@fubac.fukuyama-u.ac.jp
Oida
N
N
Urakami
T
T
Tonomura
K
K
D000421:Alcaligenes / Q000201:enzymology* / Q000235:genetics; D001673:Biodegradation, Environmental; D002265:Carboxylic Ester Hydrolases / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D008049:Lipase / Q000378:metabolism; D009154:Mutation; D011091:Polyesters / Q000378:metabolism*; D013379:Substrate Specificity
D011091:Polyesters; C016240:polycaprolactone; D002265:Carboxylic Ester Hydrolases; D008049:Lipase