Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase.
Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase.
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DOI：
10.3390/ijms19092803
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发表时间：
2018-09-18
影响因子：
5.6
通讯作者：
Jia Y
中科院分区：
文献类型：
--
作者：
Fan S;Wang J;Yan Y;Wang J;Jia Y
尽管有大量的特征性微生物能够降解邻苯二甲酸酯（PAEs），但很少有分离菌株在广泛的环境条件下对PAEs具有高活性。在本研究中，Gordonia sp. YC-JH 1在邻苯二甲酸二（2-乙基己基）酯（DEHP）降解性能方面优于其对应物。在20-50 °C、pH 5.0-12.0、0- 8%NaCl范围内，该菌具有良好的降解能力，最佳降解条件为40 °C、pH 10.0。因此，菌株YC-JH 1适合在不同条件下进行生物修复。代谢产物分析表明，菌株YC-JH 1可将DEHP依次水解为邻苯二甲酸单（2-乙基己基）酯（MEHP）和邻苯二甲酸（PA）。菌株YC-JH 1的水解酶MphG 1能水解邻苯二甲酸单乙酯（MEP）、邻苯二甲酸单丁酯（MBP）、邻苯二甲酸单己酯（MHP）和邻苯二甲酸单乙酯（MEHP）生成PA。通过对MphG 1与邻苯二甲酸单烷基酯（MAPs）的分子对接和分子动力学模拟，发现了一些关键残基，包括催化三联体（S125-H291-D259）和可能与底物结合的残基R126和F54。这些残基的突变导致活性降低。初步阐明了MphG 1催化MAPs的作用机制，为进一步研究更多水解酶的催化机制提供了理论依据。
Despites lots of characterized microorganisms that are capable of degrading phthalic acid esters (PAEs), there are few isolated strains with high activity towards PAEs under a broad range of environmental conditions. In this study, Gordonia sp. YC-JH1 had advantages over its counterparts in terms of di(2-ethylhexyl) phthalate (DEHP) degradation performance. It possessed an excellent degradation ability in the range of 20–50 °C, pH 5.0–12.0, or 0–8% NaCl with the optimal degradation condition 40 °C and pH 10.0. Therefore, strain YC-JH1 appeared suitable for bioremediation application at various conditions. Metabolites analysis revealed that DEHP was sequentially hydrolyzed by strain YC-JH1 to mono(2-ethylhexyl) phthalate (MEHP) and phthalic acid (PA). The hydrolase MphG1 from strain YC-JH1 hydrolyzed monoethyl phthalate (MEP), mono-n-butyl phthalate (MBP), mono-n-hexyl phthalate (MHP), and MEHP to PA. According to molecular docking and molecular dynamics simulation between MphG1 and monoalkyl phthalates (MAPs), some key residues were detected, including the catalytic triad (S125-H291-D259) and the residues R126 and F54 potentially binding substrates. The mutation of these residues accounted for the reduced activity. Together, the mechanism of MphG1 catalyzing MAPs was elucidated, and would shed insights into catalytic mechanism of more hydrolases.
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