Metabolism of azo dyes derived from benzidine, 3,3'-dimethylbenzidine and 3,3' -dimethoxybenzidine to potentially carcinogenic aromatic amines by intestinal bacteria

Cerniglia, Carl E.; Freeman, Jeremiah P.; Franklin, Wirt; Pack, Laura

doi:10.1093/carcin/3.11.1255

Cited by 88 publications

(40 citation statements)

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“…Azo dyes are regarded as relatively persistent pollutants because they are not readily degraded under aerobic conditions [10][11][12]. Under anaerobic conditions, azo dyes can be reduced by intestinal bacteria and some environmental microorganisms to colorless amines, which may be toxic, mutagenic, and carcinogenic to human and animals [13][14][15][16][17][18].…”

Section: Introductionmentioning

confidence: 99%

Recent Advances in Azo Dye Degrading Enzyme Research

Chen¹

2006

CPPS

219

125

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Azo dyes, which are characterized by one or more azo bonds, are a predominant class of colorants used in tattooing, cosmetics, foods, and consumer products. These dyes are mainly metabolized by bacteria to colorless aromatic amines, some of which are carcinogenic, by azoreductases that catalyze a NAD(P)H-dependent reduction. The resulting amines are further degraded aerobically by bacteria. Some bacteria have the ability to degrade azo dyes both aerobically and anaerobically. Plant-degrading white rot fungi can break down azo dyes by utilizing a number of oxidases and peroxidases as well. In yeast, a ferric reductase system participates in the extracellular reduction of azo dyes. Recently, two types of azoreductases have been discovered in bacteria. The first class of azoreductases is monomeric flavin-free enzymes containing a putative NAD(P)H binding motif at their N-termini; the second class is polymeric flavin dependent enzymes which are studied more extensively. Azoreductases from bacteria represent novel families of enzymes with little similarity to other reductases. Dissociation and reconstitution of the flavin dependent azoreductases demonstrate that the non-covalent bound flavin prosthetic group is required for the enzymatic functions. In this review, structures and carcinogenicity of azo colorants, protein structure, enzymatic function, and substrate specificity, as well as application of the azo dyes and azoreductases will be discussed.

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Section: Introductionmentioning

confidence: 99%

Recent Advances in Azo Dye Degrading Enzyme Research

Chen¹

2006

CPPS

219

125

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“…Azo dyes are used in the textile, pharmaceutical, food, and cosmetics industries. Nitro-PAHs are ubiquitous environmental contaminants that have been detected in carbon black, photocopier toners, urban air particulates, diesel fuel emissions, used motor oil, barbecued foods, and tea leaves (1)(2)(3)(4). In mammalian systems, azo dyes and nitro-PAHs are reduced to aromatic amines by enzymes from intestinal bacteria and from the liver.…”

Section: Human Intestinal Bacteriamentioning

confidence: 99%

“…The activity of azoreductase produced by each bacterial isolate can be quantified by following the rate of decrease in the absorbance of azo dye, e.g., Direct Blue 15, at 615 nm with time (2). The activity of nitroreductase produced can be determined by measuring the conversion of 4-nitrobenzoic acid to 4-aminobenzoic acid.…”

Section: Human Intestinal Bacteriamentioning

confidence: 99%

Reduction of Azo Dyes and Nitroaromatic Compounds by Bacterial Enzymes from the Human Intestinal Tract

Rafii¹,

Cerniglia²

1995

Environmental Health Perspectives

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Several anaerobic bacteria from the human intestinal tract are capable of reducing azo dyes and nitropolycyclic aromatic hydrocarbons to the corresponding aromatic amines with enzymes that have azoreductase and nitroreductase activities. The majority of bacteria with these activities belong to the genera Clostridium and Eubacterium. The azoreductases and nitroreductases from three Clostridium strains and one Eubacterium strain were studied. Both enzymes were produced constitutively in each of the bacteria; the enzymes from various bacteria had different electrophoretic mobilities. The azoreductases from all of the bacteria had immunological homology, as was evident from the cross-reactivity of an antibody raised against the azoreductase of C. perfringens with azoreductases from other bacteria. Comparison of azoreductases and nitroreductases showed that they both had identical electrophoretic mobilities on polyacrylamide gels and reacted with the antibody against the azoreductase from C. perfringens. Furthermore, the nitroaromatic compounds competitively inhibited the azoreductase activity. The data indicate that the reduction of both nitroaromatic compounds and azo dyes may be carried out by the same enzyme, which is possibly a flavin adenine dinucleotide dehydrogenase that is synthesized throughout the cell and not associated with any organized subcellular structure. -Environ Health Perspect 1 03(Suppl 5):1 7-19 (1995)

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“…It has been shown that commercially used dyes based on BZ and its derivatives can be metabolised in the human body, releasing free aminobiphenyls (Cerniglia et al, 1982). At the same time, BZ is a strong carcinogen that causes cancer in the bladder, the liver and mammary glands and also results in the development of carcinoma in the thyroid glands in animals (Sentchouk and Grintsevich, 2004).…”

Section: Introductionmentioning

confidence: 99%

Soybean peroxidase-catalysed removal of benzidines from water

Altahir

FengWei

Hassan

et al. 2015

Journal of Environmental Engineering and Science

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Crude soybean peroxidase (SBP), isolated from soybean seed coats (hulls) at unusually low concentrations, catalyses the oxidative polymerisation of hazardous aqueous benzidine and its 3,3′-dichloro, 3,3′-dimethyl and 3,3′-dimethoxy derivatives in the presence of hydrogen peroxide. The optimum operating conditions for oxidation of 0·10 mM benzidine were investigated. At pH 5, the hydrogen peroxide-to-substrate concentration ratio was 1·5 and the minimum SBP concentration required to achieve at least 95% conversion of the benzidine in synthetic wastewater was 0·43 mU/ml. Progress curves were established for the conversion of the four substrates, and apparent first-order rate constants were derived. Enzyme-catalysed polymerisation with SBP and subsequent removal of the polymeric products generated can provide an alternative means to conventional methods for treating many aromatic wastewater pollutants, including the benzidines studied here.

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Metabolism of azo dyes derived from benzidine, 3,3'-dimethylbenzidine and 3,3' -dimethoxybenzidine to potentially carcinogenic aromatic amines by intestinal bacteria

Cited by 88 publications

References 0 publications

Recent Advances in Azo Dye Degrading Enzyme Research

Recent Advances in Azo Dye Degrading Enzyme Research

Reduction of Azo Dyes and Nitroaromatic Compounds by Bacterial Enzymes from the Human Intestinal Tract

Soybean peroxidase-catalysed removal of benzidines from water

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