Accelerated degradation of dipentyl phthalate by Fusarium oxysporum f. sp. pisi cutinase and toxicity evaluation of its degradation products using bioluminescent bacteria.
The efficiency of two lipolytic enzymes (fungal cutinase and yeast esterase) in the degradation of dipentyl phthalate (DPeP) was investigated. The DPeP degradation rate of fungal cutinase was surprisingly high, i.e., almost 60% of the initial DPeP (500 mg/L) was decomposed within 2.5 hours, and nearly 40% of the degraded DPeP disappeared within the initial 15 minutes. With the yeast esterase, despite the same concentration, >87% of the DPeP remained even after 3 days of treatment. The final chemical composition after 3 days was significantly dependent on the enzyme used. During degradation with cutinase, most DPeP was converted into 1,3-isobenzofurandione (IBF) by diester hydrolysis. However, in the degradation by esterase, pentyl methyl phthalate, in addition to IBF, was produced in abundance. Toxicity monitoring using various recombinant bioluminescent bacteria showed that the degradation products from yeast esterase contained a toxic hazard, causing oxidative stress and damage to protein synthesis.
Ahn
Ji-Young
JY
Department of Chemical and Biologic Engineering, Korea University, 1,5-Ga, Anam-Dong, Sungbuk-Gu, Seoul, 136-713, South Korea.
Kim
Yang-Hoon
YH
Min
Jiho
J
Lee
Jeewon
J
D001673:Biodegradation, Environmental; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development* / Q000502:physiology; D004950:Esterases / Q000378:metabolism; D005670:Fusarium / Q000201:enzymology* / Q000378:metabolism; D049449:Luminescence; D049408:Luminescent Agents / Q000378:metabolism*; D010795:Phthalic Acids / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity; D011995:Recombination, Genetic
D049408:Luminescent Agents; D010795:Phthalic Acids; C034171:di-n-pentyl phthalate; D004950:Esterases; D002265:Carboxylic Ester Hydrolases; C019952:cutinase