1119-72-8Relevant articles and documents
Transformation of Aromatic Compounds under the Action of the Basidiomycetes Phanerochaete sanguinea and Coriolus villosus
Medvedeva, S. A.,Volchatova, I. V.,Babkin, V. A.,Antipova, I. A.,Kanitskaya, L. V.,et al.
, p. 754 - 763 (1994)
The pathways of the transformation of some aromatic compounds by the basidiomycetes Phanerochaete sanguinea and Coriolus villosus have been studied.It has been shown that the degradation of these compounds has an oxidative nature and depends on the type of substituents in the benzene ring and the propane chain.A differencew has been found in the mechanisms of the reactions of the two fungi that is a consequence of the different compositions of their enzyme complexes.
Pandell
, p. 3992,3993 (1976)
An isolated Candida albicans TL3 capable of degrading phenol at large concentration
Tsai, San-Chin,Tsai, Li-Duan,Li, Yaw-Kuen
, p. 2358 - 2367 (2005)
An isolated yeast strain was grown aerobically on phenol as a sole carbon source up to 24 mM; the rate of degradation of phenol at 30°C was greater than other microorganisms at the comparable phenol concentrations. This microorganism was further identified and is designated Candida albicans TL3. The catabolic activity of C. albicans TL3 for degradation of phenol was evaluated with the Ks and Vmax values of 1.7 ± 0.1 mM and 0.66 ± 0.02 μmol/min/mg of protein, respectively. With application of enzymatic, chromatographic and mass-spectrometric analyses, we confirmed that catechol and cis,cis-muconic acid were produced during the biodegradation of phenol performed by C. albicans TL3, indicating the occurrence of an ortho-fission pathway. The maximum activity of phenol hydroxylase and catechol-1,2-dioxygenase were induced when this strain grew in phenol culture media at 22 mM and 10 mM, respectively. In addition to phenol, C. albicans TL3 was effective in degrading formaldehyde, which is another major pollutant in waste water from a factory producing phenolic resin. The promising result from the bio-treatment of such factory effluent makes Candida albicans TL3 be a potentially useful strain for industrial application.
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Suda et al.
, (1951)
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Investigation of acid-base catalysis in the extradiol and intradiol catechol dioxygenase reactions using a broad specificity mutant enzyme and model chemistry
Brivio, Michela,Schlosrich, Janne,Ahmad, Mark,Tolond, Caroline,Bugg, Timothy D. H.
, p. 1368 - 1373 (2009)
The extradiol and intradiol catechol dioxygenase reaction mechanisms proceed via a common proximal hydroperoxide intermediate, which is processed via different Criegee 1,2-rearrangements. An R215W mutant of extradiol dioxygenase MhpB, able to produce a mi
Cloning and functional analysis of aniline dioxygenase gene cluster, from Frateuria species ANA-18, that metabolizes aniline via an ortho-cleavage pathway of catechol.
Murakami, Shuichiro,Hayashi, Teruhiko,Maeda, Tetsuya,Takenaka, Shinji,Aoki, Kenji
, p. 2351 - 2358 (2003)
Genes encoding an aniline dioxygenase of Frateuria sp. ANA-18, which metabolizes aniline via the ortho-cleavage pathway of catechol, were cloned and named tdn genes. The tdn genes were located on the chromosomal DNA of this bacterium and weren't clustered with catechol-degrading gene clusters. These results show that the ANA-18 aniline-degrading gene cluster is constructionally different from Pseudomonas tdn and Acinetobacter atd gene clusters, which degrade aniline via the meta-cleavage pathway of catechol and organize catechol-metabolic genes in the gene clusters. When cloned tdnQTA1A2B genes were expressed in Eschherichia coli, aniline dioxygenase activity was observed. Southern blot analysis revealed that homologues of the tdnA1A2B genes didn't exist in strain ANA-18. Disruption of the tdnA1A2 genes gave the parent strain ANA-18 a defect in aniline metabolism. On the basis of these results, we concluded that only the cloned tdn genes function as genes encoding aniline dioxygenase in strain ANA-18 although this bacterium had two catechol-degrading gene clusters.
Study of the paracetamol degradation pathway that generates color and turbidity in oxidized wastewaters by photo-Fenton technology
Villota, Natalia,Lomas, Jose M.,Camarero, Luis M.
, p. 113 - 119 (2016)
This study aims determining the effect that certain kind of water contaminants have on the changes of turbidity during their oxidation. Phenol is considered by its frequent presence in industrial discharges; meanwhile paracetamol is representative of emerging pollutants of pharmaceutical origin. Quite different results are observed in the turbidity changes during the oxidation of both pollutants that evolve following the kinetics of a reaction intermediate. The analysis of paracetamol and phenol degradation pathways reveals that operating conditions are important in the formation of intermediates that cause turbidity. The maximum turbidity levels are achieved operating at the ratios 12?mol HO? per 100?mg contaminant. However the turbidity generated during the paracetamol oxidation only reaches a third of the intensity achieved with phenol. During the paracetamol degradation, the intermediates causing turbidity are similar to the ones found during the phenol decomposition. These species are generated during the initial minutes of oxidation and possess structures of large size and molecular weight. At the máximum turbidity point, muconic acid and hydroquinone are identified and found to coexist with other compounds such as pyrogallol and resorcinol. Therefore, the path involving metasubstitution would be the main originator of turbidity. It is noteworthy the rapid formation of muconic acid that coexists with resorcinol-like species. These compounds enable the establishment of hydrogen bond interactions that yield supramolecular structures.
Mechanism of the Fe(III)-Catalyzed Peracetic Acid Oxidation of Catechol. A Biomimetic Reaction for Pyrocatechase
Pandell, Alexander J.
, p. 3908 - 3912 (1983)
The Fe(III)-catalyzed peracetic acid (HOOAc) oxidation of catechol to cis,cis-muconic acid (MA) is proposed as a model for the action of the Fe(III)-containing dioxygenase pyrocatechase (catechol 1,2-dioxygenase).The yield of MA is a function of the reaching a maximum of 75 percent when the ratio / is 1000.No appreciable quantity of MA is formed in the absence of Fe(III).Evidence is presented that implicates peracetic acid and hydrogen peroxide as the active oxidants and o-benzoquinone as an intermediate in the reaction.Substrate binding to Fe(III) represents an important part of the reaction.The proposed mechanism for the model involves formation of an Fe(III)-catechol complex which is oxidized to an Fe(III)-o-benzoquinone species.The Fe(III)-quinone complex then undergoes nucleophilic attack at carbonyl by H2O2 to give a peroxide addition product which undergoes intramolecular nucleophilic addition at the adjacent carbonyl to give a dioxetane intermediate.Spontaneous opening of the dioxetane gives MA.
Multi-Enzymatic Cascade Reactions for the Synthesis of cis,cis-Muconic Acid
Di Nardo, Giovanna,Gazzola, Silvia,Gilardi, Gianfranco,Pollegioni, Loredano,Rosini, Elena,Valetti, Francesca,Vignali, Elisa
, p. 114 - 123 (2021/10/07)
Lignin valorization allows the generation of a number of value-added products such as cis,cis-muconic acid (ccMA), which is widely used for the synthesis of chemicals for the production of biodegradable plastic materials. In the present work, we reported the first multi-enzymatic, one-pot bioconversion process of vanillin into ccMA. In details, we used four sequential reactions catalyzed by xanthine oxidase, O-demethylase LigM (and the tetrahydrofolate-regeneration enzyme methyl transferase MetE), decarboxylase AroY (based on the use of E. coli transformed cells) and catechol 1,2-dioxygenase CatA. The optimized lab-scale procedure allowed to reach, for the first time, the conversion of 5 mM vanillin into ccMA in ～30 h with a 90% yield: this achievement represents an improvement in terms of yields and time when compared to the use of a whole-cell system. This multi-enzymatic system represents a sustainable alternative for the production of a high value added product from a renewable resource. (Figure presented.).
Sustainable oxidative cleavage of catechols for the synthesis of muconic acid and muconolactones including lignin upgrading
Coupé, Florentin,Petitjean, Laurène,Anastas, Paul T.,Caijo, Frédéric,Escande, Vincent,Darcel, Christophe
supporting information, p. 6204 - 6211 (2020/10/18)
Muconic acid and muconolactones are attracting high interest as platform molecules for the synthesis of a variety of compounds, especially in the domain of materials. Although several technologies have been described for their synthesis, there is still a lack of performance, especially regarding green chemistry principles. In this study, we describe the development of an optimized catechol oxidative cleavage to muconic acid using performic acid in an intriguingly safe fashion. Common iron salts were used as catalysts to a level as low as 0.005 mol%, for a maximum turnover number of 13?200. Maximum muconic acid yield reached 84% after isolation by simple filtration. This procedure optimized on catechol was also efficient over a wide range of substituted catechols, providing access to muconolactones in a domino reaction. Noticeably, biobased catechols produced by a proven technology of lignin depolymerization were cleaved into muconolactones of high functional value. Applying this supplementary cleavage step to catechols obtained by lignin depolymerization was thus an ultimate way to maximize the economical value created from lignin. In contrast to other studies, lignin was not only depolymerized, but also depolymerization products were further transformed to take as much value from biomass as possible.
