Degradation Of Alkylphenols Research Articles

A laccase Gl-LAC-4 purified from white-rot fungus Ganoderma lucidum had a strong ability to degrade and detoxify the alkylphenol pollutants 4-n-octylphenol and 2-phenylphenol

In this study, the ability of laccase Gl-LAC-4, purified from Ganoderma lucidum, to degrade and detoxify two representative alkylphenol pollutants, 4-n-octylphenol and 2-phenylphenol, was systematically studied. Gl-LAC-4 laccase had a very strong ability to degrade high concentrations of 4-n-octylphenol, 2-phenylphenol, and alkylphenol mixtures. The degradation speed of Gl-LAC-4 toward 2-phenylphenol was very fast. Gl-LAC-4 displayed strong tolerance for a variety of metal salts and organic solvents in the degradation of alkylphenols. Gl-LAC-4 showed strong tolerance for high concentrations of various metal salts, such as MgSO4, MnSO4, Na2SO4, CuSO4, ZnSO4, CdSO4, and K2SO4, in the degradation of 4-n-octylphenol and 2-phenylphenol.In the case of the same metal cation, the inhibitory effect of the metal salt with Cl− as the anion on the degradation of 4-n-octylphenol and 2-phenylphenol by laccase was stronger than that of the metal salt with SO42− as the anion. An increase in the number of chloride ions caused a greater inhibitory effect on alkylphenol degradation by laccase. Gl-LAC-4 exhibited strong tolerance for glycerol, ethylene glycol, butanediol, propylene glycol, and organic solvent mixtures in the degradation of alkylphenols. Gl-LAC-4 treatment significantly reduced or eliminated the phytotoxicity of 4-n-octylphenol and 2-phenylphenol.

Activation of persulfate with dual-doped reduced graphene oxide for degradation of alkylphenols

In this study, the nitrogen and sulfur dual doped reduced graphene oxide (N,S-rGO) were synthesized using thermal decomposition strategy. And the prepared N,S-rGO could efficiently activate persulfate (PS) to generate reactive radicals for the catalytic degradation of alkylphenols at environmentally relevant concentration. The hydroxyl radicals (OH) and sulfate radicals (SO4−) generated by PS activation were analyzed by electron paramagnetic resonance (EPR). The used N,S-rGO (50 mg/L) and potassium persulfate (0.9 mmol/L) achieved complete degradation of 4-n-octylphenol, 4-n-nonylphenol and bisphenol A (20 μg/L) within 30 min at pH 6.64, exhibiting great catalytic oxidation capacity. Their final application in environmental waters turned out to be effectual as well.

Adsorption driven preferential degradation of alkyl phenols on hydrophobic perfluoroalkyl modified {0 0 1}-TiO2

Preferential degradation of low concentrated contaminants with high toxicity is of great environmental significant. Perfluoroalkyl group was adopted as functional group to construct hydrophobic surface on highly exposed {0 0 1}-TiO2 for preferential degradation of nonyl phenol. The modified electrode showed superior hydrophobicity with contact angle of more than 160° after optimization of preparation condition. Besides, the modified electrode improved light absorbance ability of visible light, leading to better photocatalytic property. The degradation of NP, OP and HP on the modified {0 0 1}-TiO2 was obviously more efficient over that unmodified, which was about 1.5 times in the kinetic constant, showing preferential degradation of alkyl phenols on perfluoroalkyl decorated {0 0 1}-TiO2. Preferential degradation on the modified {0 0 1}-TiO2 was due to the superior adsorption ability to alkyl phenols. The adsorption capacity to alkyl phenols on the modified electrode was more than 2 times over the that unmodified. The adsorption of alkyl phenols on the hydrophobic electrode was further studied by in-situ infrared. It was found that there was specific hydrophobic interaction between the alkyl group of alkyl phenols and the perfluoroalkyl group modified on photocatalyst surface, which was the reason of alkyl phenols preferential degradation on the hydrophobic photocatalytic interface. The results showed great potential applications in selective wastewater treatment.

Molecular Characterization of Polythene Degrading Soil Microbe, Bacillus Cereus NAIMCC-B-01818

Pollution of soil and water by polyethylene, a saturated hydrocarbon and commonly known as polythene is a major threat to environment and human health in recent times. Several microorganisms occurring in the natural ecosystems are capable of degrading polythene. Biodegrading microbes were isolated from contaminated soil of IARI campus and a total of 12 isolates were screened for their ability to degrade polythene. Biodegradation was measured by mean weight loss of the polythene piece grown in the presence of the liquid culture of the microbial isolates for 30 days. 3% degradation of polythene was observed by the microbial isolate PL12. Based on biodegradation efficiency, PL12 was selected for further characterization and molecular studies. The microbial isolate PL12 was observed as rod-shaped gram positive bacterium. Carbohydrate utilization test confirmed the isolate PL12 to Bacillus genus and it was analyzed to be tolerant to alkaline (upto pH 10.0) and moderately high osmotic (2% sodium chloride) conditions. Further, 16S rDNA amplification and sequencing identified microbial isolate PL12 as Bacillus cereus. Using gene specific primers successful amplification of alkB (alkane monooxygenase B) gene was obtained in the isolate PL12, confirming the presence of alkylphenol degradation metabolic pathway in the isolate PL12.

Fate and metabolism of the brominated flame retardant tetrabromobisphenol A (TBBPA) in rice cell suspension culture

Tetrabromobisphenol A (TBBPA) is the brominated flame retardant with the highest production volume and its bioaccumulation in environment has caused both human health and environmental concerns, however the fate and metabolism of TBBPA in plants is unknown. We studied the fate, metabolites, and transformation of 14C-labeled TBBPA in rice cell suspension culture. During the incubation for 14 days, TBBPA degradation occurred continuously in the culture, accompanied by formation of one anisolic metabolite [2,6-dibromo-4-(2-(2-hydroxy)-propyl)-anisole] (DBHPA) (50% of the degraded TBBPA) and cellular debris-bound residues (46.4%) as well as mineralization (3.6%). The cells continuously accumulated TBBPA in the cytoplasm, while a small amount of DBHPA (2.1% of the initially applied TBBPA) was detectable inside the cells only at the end of incubation. The majority of the accumulated residues in the cells was attributed to the cellular debris-bound residues, accounting for 70–79% of the accumulation after the first incubation day. About 5.4% of the accumulation was associated with cell organelles, which contributed 7.5% to the cellular debris-bound residues. Based on the fate and metabolism of TBBPA in the rice cell suspension culture, a type II ipso-substitution pathway was proposed to describe the initial step for TBBPA degradation in the culture and balance the fate of TBBPA in the cells. To the best of our knowledge, our study provides for the first time the insights into the fate and metabolism of TBBPA in plants and points out the potential role of type II ipso-hydroxylation substitution in degradation of alkylphenols in plants. Further studies are required to reveal the mechanisms for the bound-residue formation (e.g., binding of residues to specific cell wall components), nature of the binding, and toxicological effects of the bound residues and DBHPA.

Catabolism of 4-alkylphenols by Acinetobacter sp. OP5: Genetic organization of the oph gene cluster and characterization of alkylcatechol 2, 3-dioxygenase

In this study, a specific PCR primer set was successfully designed for alkylcatechol 2, 3-dioxygenase genes and applied to detect the presence of this biomarker in 4-t-octylphenol-degrading Acinetobacter sp. strain OP5. A gene cluster (ophRBA1A2A3A4A5A6CEH) encoding multicomponent phenol hydroxylase and alkylcatechol 2, 3-dioxygenase was then cloned from this strain and showed the highest homology to those involved in the published medium-chain alkylphenol gene clusters. The pure enzyme of recombinant cell harboring ophB showed meta-cleavage activities for 4-methylcatechol (1,435%), 4-ethylcatechol (982%), catechol (100%), 4-t-butylcatechol (16.6%), and 4-t-octylcatechol (3.2%). The results suggest that the developed molecular technique is useful and easy in detection of medium/long-chain alkylphenol degradation gene cluster. In addition, it also provides a better understanding of the distribution of biodegradative genes and pathway for estrogenic-active long-chain alkylphenols in bacteria.

Application of Titanium Dioxide‐Graphene Composite Material for Photocatalytic Degradation of Alkylphenols

Titanium dioxide‐graphene (TiO2‐G) composite was used for the photodegradation of alkylphenols in wastewater samples. The TiO2‐G composites were prepared via sonochemical and calcination methods. The synthesized composite was characterized by X‐ray diffraction (XRD), infrared spectroscopy (IR), scanning electron microscopy (SEM), transmission electron microscopy (TEM), energy dispersive X‐ray analysis (EDX), and fluorescence spectroscopy. The photocatalytic efficiency was evaluated by studying the degradation profiles of alkylphenols using gas chromatography‐flame ionization detector (GC‐FID). It was found that the synthesized TiO2‐G composites exhibit enhanced photocatalytic efficiencies as compared to pristine TiO2. The presence of graphene not only provides a large surface area support for the TiO2 photocatalyst, but also stabilizes charge separation by trapping electrons transferred from TiO2, thereby hindering charge transfer and enhancing its photocatalytic efficiency.

Degradation of Alkylphenols by White Rot Fungus Irpex lacteus and Its Manganese Peroxidase

Alkylphenols are common endocrine disrupters that are produced from the degradation of widely used surfactants. Since they cause various harmful effects on aquatic life and in humans, they should be removed from the environments being contaminated. White rot fungus Irpex lacteus can completely degrade 100 mg/L of octylphenol, nonylphenol, and phenylphenol during 1 day of incubation in the complex YMG medium, which was the highest degrading capability among nine strains of white rot fungi tested. In the N-limited Kirk's basal salts medium, I. lacteus could degrade almost 100 % of 100 mg/L octylphenol and nonylphenol in 1 h, and exhibited a high activity of manganese peroxidase (MnP; 1,790 U/L). MnP of I. lacteus was purified by ion exchange chromatography, and this degraded 99 % of 50 mg/L octylphenol and removed 80 % of estrogenic activity in 2 hours. In addition, the purified MnP (10 U/mL) degraded over 90 % of 50 mg/L nonylphenol in 1 h.

Identification of the flavin monooxygenase responsible for ipso substitution of alkyl and alkoxyphenols in Sphingomonas sp. TTNP3 and Sphingobium xenophagum Bayram

We previously showed that opdA from Sphingomonas sp. PWE1 encodes a putative flavin monooxygenase capable of transforming octylphenol (OP) via type II ipso substitution. Here, we demonstrate that an opdA homolog is responsible for OP and related alkyl/alkoxyphenol degradation in the nonylphenol degrader Sphingomonas sp. TTNP3. PCR and Southern blot analyses revealed that TTNP3 contained an opdA homolog, while a TTNP3 derivative unable to grow on nonylphenol (TTNP3d) did not. OpdA expression was confirmed in wild-type TTNP3 via two dimensional gel electrophoresis. Activity was restored to TTNP3d following complementation with opdA. Sequence analysis of an opdA homolog from another nonylphenol degrader, Sphingobium xenophagum Bayram, revealed that the predicted protein sequences from PWE1 and Bayram were identical, but differed from TTNP3 by four amino acids. In order to assess differences, we heterologously expressed the two unique opdA homologs and compared their effect on the disappearance of five alkyl/alkoxyphenol substrates and subsequent appearance of hydroquinone. For all substrates, except OP, the levels of substrate disappearance and hydroquinone appearance were significantly lower in cultures expressing odpA (TTNP3) than those expressing opdA (PWE1/Bayram). These differences in substrate specificity were consistent with an in silico model which predicted that two of the amino acid differences between odpA (TTNP3) and opdA (PWE1/Bayram) lay in a putative substrate binding pocket. While these strains are known to use the same type II ipso substitution mechanism for alkylphenol degradation, this work provides the first preliminary evidence that opdA homologs also encode the type I ipso substitution activity responsible for the degradation of alkoxyphenols.

An unexpected gene cluster for downstream degradation of alkylphenols in Sphingomonas sp. strain TTNP3

In silico analysis of nucleotide sequences flanking the recently found hydroquinone dioxygenase in Sphingomonas sp. strain TTNP3 revealed a gene cluster that encodes a hydroquinone catabolic pathway. In addition to the two open-reading frames encoding the recently characterized hydroquinone dioxygenase, the cluster consisted of six open-reading frames. We were able to express the three open-reading frames, hqdC, hqdD, and hqdE, and demonstrated that the three gene products, HqdC, HqdD, and HqdE had 4-hydroxymuconic semialdehyde dehydrogenase, maleylacetate reductase, and intradiol dioxygenase activity, respectively. Surprisingly, the gene cluster showed similarities to functionally related clusters found in members of the β- and γ-proteobacteria rather than to those found in other members of the genus Sphingomonas sensu latu.

Purification and characterization of hydroquinone dioxygenase from Sphingomonas sp. strain TTNP3

Hydroquinone-1,2-dioxygenase, an enzyme involved in the degradation of alkylphenols in Sphingomonas sp. strain TTNP3 was purified to apparent homogeneity. The extradiol dioxygenase catalyzed the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones. The activity of 1 mg of the purified enzyme with unsubstituted hydroquinone was 6.1 μmol per minute, the apparent Km 2.2 μM. ICP-MS analysis revealed an iron content of 1.4 moles per mole enzyme. The enzyme lost activity upon exposure to oxygen, but could be reactivated by Fe(II) in presence of ascorbate. SDS-PAGE analysis of the purified enzyme yielded two bands of an apparent size of 38 kDa and 19 kDa, respectively. Data from MALDI-TOF analyses of peptides of the respective bands matched with the deduced amino acid sequences of two neighboring open reading frames found in genomic DNA of Sphingomonas sp strain TTNP3. The deduced amino acid sequences showed 62% and 47% identity to the large and small subunit of hydroquinone dioxygenase from Pseudomonas fluorescens strain ACB, respectively. This heterotetrameric enzyme is the first of its kind found in a strain of the genus Sphingomonas sensu latu.

Degradation of alkylphenols in the presence of riboflavin under near-ultraviolet light

Degradation of alkylphenols in the presence of riboflavin under near-ultraviolet light

Catalytic Oxidative Domino Degradation of Alkyl Phenols Towards 2- and 3-Substituted Muconolactones

The catalytic oxidative domino degradation of phenols was investigated. Hydrogen peroxide (30% aq.) was used as an oxidant and 2,2′-dinitro-4,4′-ditrifluoromethyldiphenyl diselenide 4e as a catalyst. The products were muconic acid 5, and muconolactones muconolactones—5-carboxymethylfuran-2(5H)-ones 7 and 9. Phenols with alkyl groups at 2 or 4 positions of the benzene ring were converted regioselectively to corresponding muconolactones substituted at alkenylene ring carbon atoms. The reaction mechanism is proposed.

Anaerobic biodegradation of 4-alkylphenols in a paddy soil microcosm supplemented with nitrate

Anaerobic degradation of phenol, p-cresol, 4- n-propylphenol ( n-PP), 4- i-propylphenol ( i-PP), 4- n-butylphenol ( n-BP) and 4- sec-butylphenol ( sec-BP) was observed in a paddy soil supplemented with nitrate. We detected the metabolites 4′-hydroxypropiophenone (HPP) from n-PP, 4- i-propenylphenol from i-PP, and 4-(1-butenyl)phenol and 4′-hydroxybutyrophenone (HBP) from n-BP. Compared with the original soils, Betaproteobacteria became predominant in the microcosm during the degradation of phenol and p-cresol whereas no remarkable change was observed in the community degrading propylphenols and butylphenols. The microcosm, however, did not degrade 4- t-butylphenol ( t-BP), 4- t-octylphenol ( t-OP) and 4- n-octylphenol ( n-OP). Paddy soil supplemented with sulfate or iron (III) as electron acceptors did not degrade phenol and 4-alkylphenols with the exception of the degradation of p-cresol in sulfate-reducing conditions. It was demonstrated for the first time that anaerobic microbial degradation of alkylphenols, in a paddy soil supplemented with nitrate as an electron acceptor, occurred via oxidation of the alpha carbon in the alkyl chain.

Characterization of alkylphenol degradation gene cluster in Pseudomonas putida MT4 and evidence of oxidation of alkylphenols and alkylcatechols with medium-length alkyl chain

Alkylphenols (APs) are ubiquitous contaminants in aquatic environments and have endocrine disrupting and toxic effects on aquatic organisms. To investigate biodegradation mechanisms of APs, an AP degradation gene cluster was cloned from a butylphenol (BP)-degrading bacterium, Pseudomonas putida MT4. The gene cluster consisted of 13 genes named bupBA1A2A3A4A5A6CEHIFG. From the nucleotide sequences, bupA1A2A3A4A5A6 were predicted to encode a multicomponent phenol hydroxylase (PH), whereas bupBCEHIFG were expected to encode meta-cleavage pathway enzymes. A partial sequence of a putative NtrC-type regulatory gene, bupR, was also found upstream of the gene bupB. This result indicates that APs can be initially oxidized into alkylcatechols (ACs), followed by the meta-cleavage of the aromatic rings. To confirm this pathway, AP degradation tests were carried out using the recombinant P. putida KT2440 harboring the PH genes (bupA1A2A3A4A5A6). The recombinant strain oxidized 4-n-APs with an alkyl chain of up to C7 (< or = C7) efficiently and also several BPs including those with an alkyl chain with some degree of branching. Therefore, it was found that PH had a broad substrate specificity for APs with a medium-length alkyl chain (C3-C7). Moreover, the cell extract of a recombinant Escherichia coli harboring bupB (a catechol 2,3-dioxygenase gene) converted 4-n-ACs with an alkyl chain of < or = C9 into yellow meta-cleavage products with a maximum absorbance at 379 nm, indicating that the second step enzyme in this pathway is also responsible for the degradation of ACs with a medium-length alkyl chain. These results suggest that MT4 is a very useful strain in the biodegradation of a wide range of APs with a medium-length alkyl chain, which known nonylphenol-degrading Sphingomonas strains have never degraded.

Oxidative Degradation of Alkylphenols by Horseradish Peroxidase

Oxidative Degradation of Alkylphenols by Horseradish Peroxidase

Oxidative degradation of alkylphenols by horseradish peroxidase

Alkylphenols such as bisphenol A (2,2-bis(4-hydroxyphenyl)propane; BPA), p-nonylphenol ( p-NP), and p-octylphenol ( p-OP) that are known as endocrine disrupters were oxidized by horseradish ( Armoracia rusticana) peroxidase (HRP) with H 2O 2. The optimal pHs for BPA, p-NP, and p-OP were 8.0, 7.0, and 5.0, respectively. The optimal temperature for BPA was 20°C. Although BPA was rapidly degraded by HRP, its degradation depended on the concentration of HRP. Most of the oxidation products of BPA were polymers, although some 4-isopropenylphenol was produced. When male Japanese medaka ( Oryzias latipes) were exposed to BPA, vitellogenin in the blood increased. However, no increased vitellogenin was observed in medaka exposed to HRP-oxidized BPA. The enzymatic oxidation of BPA using HRP was able to eliminate its estrogen-like activity.

Sonolysis of alkylphenols in aqueous solution with Fe(II) and Fe(III)

The sonolytic degradation of alkylphenols (APs), such as butylphenol, pentylphenol, octylphenol, and nonylphenol (NP), in water was investigated at a sound frequency of 200 kHz with an acoustic intensity of 6 W cm −2 under argon, oxygen, and air atmospheres. The sonolytic degradation rate of the APs under the conditions of the present study depended upon their alkyl chain length. The decrease in the degradation rate by the radical scavenging effect was in the range of about 48–82% for APs in the presence of 3 mM 2-methyl-2-propanol. The free radicals play a significant role in the sonolytic degradation process of the APs. In the presence of Fe(II) and Fe(III), the pseudo-first-order rate constants for the sonolytic degradation of 30 μM NP as a function of the concentration of Fe(II) and Fe(III) were estimated under argon and oxygen. The maximum rate constants were observed at 50 μM Fe(II) (0.139±0.008 min −1) and 100 μM Fe(III) (0.103±0.001 min −1) under oxygen. The total organic carbon concentration (TOC) was investigated under same conditions. TOC decreased in the range of about 50–70% during the sonication in the presence of Fe(II) and Fe(III) under argon and oxygen. The sonochemical effects by the addition of Fe(II) and Fe(III) as catalyst during the sonication under the proper atmosphere result in a remarkable enhancement of degradation and mineralization.

Embryotoxicity of the Alkylphenol Degradation Product 4-Nonylphenol to the Crustacean Daphnia magna

Laboratory studies have suggested that some alkylphenols and pesticides elicit developmental toxicity to crustaceans. The purpose of the present study was to evaluate the possibility that the alkylphenol degradation product 4-nonylphenol is embryotoxic to the crustacean Daphnia magna through its known ability to interfere with the metabolic elimination of testosterone. Direct exposure of maternal daphnids to testosterone caused developmental abnormalities in neonates that consisted of partial arrest of early embryonic development and abnormalities in shell spine and first antennae development. Exposure of maternal daphnids to concentrations of 4-nonylphenol also produced developmental abnormalities though the profile of abnormalities was distinct from that observed throughout the testosterone concentration-response curve. Thus, 4-nonylphenol is a developmental toxicant in daphnids, but its toxicity is not consistent with that elicited by elevated testosterone accumulation. Further experiments demonstrated that testosterone was directly toxic to developing embryos, and the maternal organism can serve as the vector for this toxicity. In contrast, neither direct embryo exposure nor early maternal exposure to 4-nonylphenol elicited embryotoxicity consistent with that observed during continuous maternal and gestational exposure. Thus, 4-nonylphenol is not directly embryotoxic at these exposure levels, but rather toxicity is mediated by maternal influences during gestation. The threshold concentration for the occurrence of developmental abnormalities ( approximately 44 microg/L) indicates that typical environmental concentrations of 4-nonylphenol pose no imminent hazard with respect to developmental toxicity. However, these effects do occur at sufficiently low levels to warrant evaluation of the relative susceptibility of other crustacean species to this previously uncharacterized mode of toxicity.

Embryotoxicity of the alkylphenol degradation product 4-nonylphenol to the crustacean Daphnia magna.

Laboratory studies have suggested that some alkylphenols and pesticides elicit developmental toxicity to crustaceans. The purpose of the present study was to evaluate the possibility that the alkylphenol degradation product 4-nonylphenol is embryotoxic to the crustacean Daphnia magna through its known ability to interfere with the metabolic elimination of testosterone. Direct exposure of maternal daphnids to testosterone caused developmental abnormalities in neonates that consisted of partial arrest of early embryonic development and abnormalities in shell spine and first antennae development. Exposure of maternal daphnids to concentrations of 4-nonylphenol also produced developmental abnormalities though the profile of abnormalities was distinct from that observed throughout the testosterone concentration-response curve. Thus, 4-nonylphenol is a developmental toxicant in daphnids, but its toxicity is not consistent with that elicited by elevated testosterone accumulation. Further experiments demonstrated that testosterone was directly toxic to developing embryos, and the maternal organism can serve as the vector for this toxicity. In contrast, neither direct embryo exposure nor early maternal exposure to 4-nonylphenol elicited embryotoxicity consistent with that observed during continuous maternal and gestational exposure. Thus, 4-nonylphenol is not directly embryotoxic at these exposure levels, but rather toxicity is mediated by maternal influences during gestation. The threshold concentration for the occurrence of developmental abnormalities ( approximately 44 microg/L) indicates that typical environmental concentrations of 4-nonylphenol pose no imminent hazard with respect to developmental toxicity. However, these effects do occur at sufficiently low levels to warrant evaluation of the relative susceptibility of other crustacean species to this previously uncharacterized mode of toxicity.