Enzymatic degradation of dibutyl phthalate and toxicity of its degradation products.
Dibutyl phthalate (DBP) was more efficiently degraded by cutinase compared to yeast esterase; i.e. almost 80% of initial DBP (500 mg l(-1)) was decomposed within 7.5 h, and nearly 50% of the degraded DBP disappeared within the initial 30 min. The toxicity of the final DBP degradation products were investigated using various recombinant bioluminescent bacteria. Butyl methyl phthalate, the major product of degradation by the esterase, was an oxidative toxic hazard that damaged protein synthesis.
Kim
Yang-Hoon
YH
Department of Chemical and Biological Engineering, Korea University, 1, 5-Ka, Anam-Dong, Sungbuk-Ku, Seoul 136-713, South Korea.
Lee
Jeewon
J
D001419:Bacteria / Q000378:metabolism; D001673:Biodegradation, Environmental; D001709:Biotechnology / Q000379:methods*; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism; D003993:Dibutyl Phthalate / Q000737:chemistry* / Q000633:toxicity; D004926:Escherichia coli / Q000378:metabolism; D004950:Esterases / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry; D008401:Gas Chromatography-Mass Spectrometry; D049449:Luminescence; D008956:Models, Chemical; D010100:Oxygen / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D013997:Time Factors
D005656:Fungal Proteins; D011994:Recombinant Proteins; D003993:Dibutyl Phthalate; D004950:Esterases; D002265:Carboxylic Ester Hydrolases; C019952:cutinase; D010100:Oxygen