Biodegradation of phthalic acid esters (PAEs) by Cupriavidus oxalaticus strain E3 isolated from sediment and characterization of monoester hydrolases. (March 2021)

• Record Type: Journal Article
• Authors: Chen, Fangyuan; Li, Xuli; Dong, Yiqie; Li, Jiahao; Li, Yixin; Li, He; Chen, Lei; Zhou, Min; Hou, Haobo
• Is Part Of: Chemosphere. Volume 266(2021)
• Publication Date: 2021-03
• Subjects: Plasticizers -- Transformation pathway -- Genome sequencing -- Catalytic triplet; Pollution -- Periodicals; Pollution -- Physiological effect -- Periodicals; Environmental sciences -- Periodicals; Atmospheric chemistry -- Periodicals; 551.511
• DOI: 10.1016/j.chemosphere.2020.129061
• Languages: English
• ISSNs: 0045-6535

Abstract

Abstract: Phthalic acid esters (PAEs) are teratogenic and carcinogenic and mainly metabolized by microorganisms in sediment. A novel strain, Cupriavidus oxalaticus strain E3, was isolated and characterized from sediment for PAEs degradation. The transformation of dibutyl phthalate (DBP) and bis(2-ethylhexyl) phthalate (DEHP) as the sole carbon source by strain E3 was systematically studied in the darkness through the kinetic studies and analysis of intermediates. After the initial lag pause of 5 h–8 h, the strain efficiently degraded 87.4%–94.4% of DBP and 82.5%–85.6% of DEHP at an initial amount of each phthalate of 200 mg/L after 60 h of incubation. The biodegradation rate of DBP and DEHP followed a first-order kinetic model, and degradation rate constants (k) of them by E3 were 1.37 and 0.86 d −1, respectively. Gas chromatography–mass spectrometry (GC–MS) results revealed that the tentative PAEs degradation pathway, included the transformation from PAEs to phthalic acid (PA) and the complete mineralization of PA. In the phase of PAEs to PA, DBP with short sides reduced the chain length via hydrolyzation, and DEHP with long sides reduced the chain length via hydrolyzation and β-oxidation. The 3D model of monoester hydrolase from C. oxalaticus was predicted and used for docking with mono-2-ethylhexyl phthalate (MEHP) and mono-n-butyl phthalate (MBP). The docking results showed that the conserved catalytic triplet structure (Ser140, His284, and Asp254) acted as active sites and participated in degrading PMEs. This study provided novel insights into the mechanisms of PAEs degradation at a molecular level and widened the scope of functional bacteria by isolating strain E3. Graphical abstract: Image 1 Highlights: A novel strain isolated as PAEs-degrading microorganisms. The main metabolites of PAEs were identified. The differences of pathways and metabolites of PAEs with different side chains length were studied. The mechanism of PME hydrolase was analyzed. Monoester hydrolases possess the catalytic triplet as active site in the catabolism of PME.