Two endocrine disrupting dibutyl phthalate degrading esterases and their compensatory gene expression in Sphingobium sp. SM42

Whangsuk, Wirongrong; Sungkeeree, Pareenart; Nakasiri, Monnapa; Thiengmag, Sirinthra; Mongkolsuk, Skorn; Loprasert, Suvit

doi:10.1016/j.ibiod.2014.12.006

Cited by 57 publications

(33 citation statements)

References 32 publications

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“…JQ478494) from Sphingobium sp. SM42 [ 14 ], respectively at high coverage. Cloning and expression of these putative esterases and hydrolases would be helpful for better understanding the mechanism of PAEs-degradation in genus Gordonia .…”

Section: Resultsmentioning

confidence: 99%

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Characterization and Genomic Analysis of a Highly Efficient Dibutyl Phthalate-Degrading Bacterium Gordonia sp. Strain QH-12

Jin

Kong

Liu

et al. 2016

IJMS

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A bacterial strain QH-12 isolated from activated sludge was identified as Gordonia sp. based on analysis of 16S rRNA gene sequence and was found to be capable of utilizing dibutyl phthalate (DBP) and other common phthalate esters (PAEs) as the sole carbon and energy source. The degradation kinetics of DBP under different concentrations by the strain QH-12 fit well with the modified Gompertz model (R2 > 0.98). However, strain QH-12 could not utilize the major intermediate product phthalate (phthalic acid; PA) as the sole carbon and energy source, and only a little amount of PA was detected. The QH-12 genome analysis revealed the presence of putative hydrolase/esterase genes involved in PAEs-degradation but no phthalic acid catabolic gene cluster was found, suggesting that a novel degradation pathway of PAEs was present in Gordonia sp. QH-12. This information will be valuable for obtaining a more holistic understanding on diverse genetic mechanisms of PAEs-degrading Gordonia sp. strains.

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Section: Resultsmentioning

confidence: 99%

“…[ 8 ], and Sphingobium sp. SM42 [ 14 ]. Most of these reported strains could only transform PAEs to their corresponding monoesters of phthalate or phthalic acid.…”

Section: Introductionmentioning

confidence: 99%

Characterization and Genomic Analysis of a Highly Efficient Dibutyl Phthalate-Degrading Bacterium Gordonia sp. Strain QH-12

Jin

Kong

Liu

et al. 2016

IJMS

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“…Apart from industrial application, esterases are the key enzymes in the degradation of estrogenic phthalate esters, one of the most abundant groups of man-made environmental pollutants, accounting for a number of potential causes of human health problems including developmental and testicular toxicity as well as exhibiting antiandrogenic, teratogenic, and carcinogenic effects [24,25]. Although there are numerous reports on the metabolism of phthalate mono-and diesters in bacteria [26][27][28][29][30], genetic information on phthalate esterases/ hydrolases that catalyzes the first step in the degradation of phthalate ester is quite limited. As far as metabolism of phthalate esters is concerned, there are only a few reports on the purified dialkyl phthalate esterase enzymes, which are capable of specifically hydrolyzing only one of the ester bonds of the diester to generate the corresponding monoalkyl phthalate esters [28,[30][31][32][33][34][35].…”

Section: Introductionmentioning

confidence: 99%

“…Although there are numerous reports on the metabolism of phthalate mono-and diesters in bacteria [26][27][28][29][30], genetic information on phthalate esterases/ hydrolases that catalyzes the first step in the degradation of phthalate ester is quite limited. As far as metabolism of phthalate esters is concerned, there are only a few reports on the purified dialkyl phthalate esterase enzymes, which are capable of specifically hydrolyzing only one of the ester bonds of the diester to generate the corresponding monoalkyl phthalate esters [28,[30][31][32][33][34][35]. On the other hand, there are only limited reports of specific monoalkyl phthalate esterases that hydrolyze monoalkyl phthalates to furnish phthalic acid but are incapable of hydrolyzing phthalate diesters [5,[36][37][38][39][40].…”

Section: Introductionmentioning

confidence: 99%

Characterization of a novel family VIII esterase EstM2 from soil metagenome capable of hydrolyzing estrogenic phthalates

et al. 2020

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Background: Microbes are rich sources of enzymes and esterases are one of the most important classes of enzymes because of their potential for application in the field of food, agriculture, pharmaceuticals and bioremediation. Due to limitations in their cultivation, only a small fraction of the complex microbial communities can be cultured from natural habitats. Thus to explore the catalytic potential of uncultured organisms, the metagenomic approach has turned out to be an effective alternative method for direct mining of enzymes of interest. Based on activity-based screening method, an esterase-positive clone was obtained from metagenomic libraries. Results: Functional screening of a soil metagenomic fosmid library, followed by transposon mutagenesis led to the identification of a 1179 bp esterase gene, estM2, that encodes a 392 amino acids long protein (EstM2) with a translated molecular weight of 43.12 kDa. Overproduction, purification and biochemical characterization of the recombinant protein demonstrated carboxylesterase activity towards short-chain fatty acyl esters with optimal activity for p-nitrophenyl butyrate at pH 8.0 and 37 °C. Amino acid sequence analysis and subsequent phylogenetic analysis suggested that EstM2 belongs to the family VIII esterases that bear modest similarities to class C β-lactamases. EstM2 possessed the conserved S-x-x-K motif of class C β-lactamases but did not exhibit β-lactamase activity. Guided by molecular docking analysis, EstM2 was shown to hydrolyze a wide range of di-and monoesters of alkyl-, aryl-and benzyl-substituted phthalates. Thus, EstM2 displays an atypical hydrolytic potential of biotechnological significance within family VIII esterases. Conclusions: This study has led to the discovery of a new member of family VIII esterases. To the best of our knowledge, this is the first phthalate hydrolase (EstM2), isolated from a soil metagenomic library that belongs to a family possessing β-lactamase like catalytic triad. Based on its catalytic potential towards hydrolysis of both phthalate diesters and phthalate monoesters, this enzyme may find use to counter the growing pollution caused by phthalatebased plasticizers in diverse geological environment and in other aspects of biotechnological applications.

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“…To date, the gene sequences of some dialkyl phthalate hydrolases have been identified, and their hydrolytic activity have been characterized. These hydrolases include M673 [ 20 ], EstS1 [ 21 ], M11 [ 22 ], DphB [ 23 ], EstG [ 24 ], and EstSP1 [ 25 ]. There are only three monoalkyl phthalate hydrolases with the gene sequence available: P8219 MehpH [ 26 ], EG-5 MehpH [ 27 ], and PatE [ 28 ].…”

Section: Introductionmentioning

confidence: 99%

Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase

Fan¹,

Wang²,

Yan³

et al. 2018

IJMS

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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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Two endocrine disrupting dibutyl phthalate degrading esterases and their compensatory gene expression in Sphingobium sp. SM42

Cited by 57 publications

References 32 publications

Characterization and Genomic Analysis of a Highly Efficient Dibutyl Phthalate-Degrading Bacterium Gordonia sp. Strain QH-12

Characterization and Genomic Analysis of a Highly Efficient Dibutyl Phthalate-Degrading Bacterium Gordonia sp. Strain QH-12

Characterization of a novel family VIII esterase EstM2 from soil metagenome capable of hydrolyzing estrogenic phthalates

Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase

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