期刊
CHEMOSPHERE
卷 288, 期 -, 页码 -出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.chemosphere.2021.132491
关键词
DEP; SOD; Biotransformation; Activity inhibition; Binding interactions
资金
- Ministry of Science and Technology of the People's Republic of China [2020YFC1808602]
- National Key Research and Development Program of China [2018YFC1801005]
- National Natural Science Foundation of China [41977356, 21377138]
- Frontier Project of Knowledge Innovation Engineering Field and 135 plans of CAS [ISSASIP1618]
The study illustrated the biotransformation of DEP into MEP and PA in earthworms, driven by endogenous carboxylesterase. MEP showed higher inhibition of SOD activity than DEP, with PA having even stronger inhibition effect. The direct binding interaction with SOD, causing conformational changes, was believed to underlie inhibition efficiency of SOD activity.
Phthalic acid esters (PAEs) are used as plasticizer or modifier in artificially-manufactured products. Though the rapid biotransformation of phthalates in microbes and plants have been well documented, it is less studied yet in terrestrial animals, e.g. earthworm. In this study, the major biotransformation of diethyl phthalate (DEP) in Eisenia fetida was illustrated using in vitro incubation of earthworm crude enzymes. DEP could be substantially biotransformed into phthalate monoester (MEP) and a small amount of phthalic acid (PA) through esterolysis, which was verified to be driven by endogenous carboxylesterase. Despite the inferior contribution, the oxidation of DEP might also occur under the initiated electron transfer by NADPH coenzyme. The dominant metabolite MEP showed a higher inhibition of superoxide dismutase (SOD) activity than DEP with EC50 of 0.0082 +/- 0.0016 mmol/L, so the higher ecological risks of MEP would be marked. The inhibition effect of PA was validated to be even stronger than MEP though it was slightly generated. The direct binding interaction with SOD was proved to be an important molecular event for regulation of SOD activity. Besides the static quenching mechanism, the caused conformational changes including despiralization of alpha-helix and spatial reorientation of tryptophan were spectrally believed to affect binding and underlie inhibition efficiency of SOD activity.
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