Identification, Isolation and characterization of a novel azoreductase from Clostridium perfringens

Morrison, J.; Wright, Cristee M.; John, Gilbert H.

doi:10.1016/j.anaerobe.2011.12.006

Cited by 58 publications

(32 citation statements)

References 18 publications

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“…Typically, they contain either flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) having an isoalloxazine ring system, which enables them to catalyze one and two electron transfer reactions (Hefti et al, 2003). Recently, a strictly anaerobic azoreductase enzyme was also characterized from Clostridium perfringens by Morrison et al (2012). The enzyme activity was highest in the presence of two cofactors, NADH and FAD.…”

Section: Structure and Function Of Dye-degrading Enzymesmentioning

confidence: 99%

Bacterial diversity and composition in major fresh produce growing soils affected by physiochemical properties and geographic locations

Ibekwe

Yang

et al. 2016

Science of The Total Environment

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Azo dyes and their intermediate degradation products are common contaminants of soil and groundwater in developing countries where textile and leather dye products are produced. The toxicity of azo dyes is primarily associated with their molecular structure, substitution groups and reactivity. To avoid contamination of natural resources and to minimize risk to human health, this wastewater requires treatment in an environmentally safe manner. This manuscript critically reviews biological treatment systems and the role of bacterial reductive and oxidative enzymes/processes in the bioremediation of dye-polluted wastewaters. Many studies have shown that a variety of culturable bacteria have efficient enzymatic systems that can carry out complete mineralization of dye chemicals and their metabolites (aromatic compounds) over a wide range of environmental conditions. Complete mineralization of azo dyes generally involves a two-step process requiring initial anaerobic treatment for decolorization, followed by an oxidative process that results in degradation of the toxic intermediates that are formed during the first step. Molecular studies have revealed that the first reductive process can be carried out by two classes of enzymes involving flavin-dependent and flavin-free azoreductases under anaerobic or low oxygen conditions. The second step that is carried out by oxidative enzymes that primarily involves broad specificity peroxidases, laccases and tyrosinases. This review focuses, in particular, on the characterization of these enzymes with respect to their enzyme kinetics and the environmental conditions that are necessary for bioreactor systems to treat azo dyes contained in wastewater.

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Section: Structure and Function Of Dye-degrading Enzymesmentioning

confidence: 99%

Bacterial diversity and composition in major fresh produce growing soils affected by physiochemical properties and geographic locations

Ibekwe

Yang

et al. 2016

Science of The Total Environment

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“…What we know from previous work performed on C. perfringens and AzoC shows that C. perfringens constitutively expresses a unique azoreductase (AzoC), specific for large azo dyes, and that sulfonated azo dyes release AzoC from the cell upon dye exposure (Morrison et al, 2012(Morrison et al, , 2014Morrison & John, 2013, 2015. It appears as though AzoC is the major azoreductase produced; however, additional azoreductases are likely generated (Morrison et al, 2012(Morrison et al, , 2014Morrison & John, 2013, 2015. The outcome of this study provides new information regarding the broad specificity of C. perfringens for a selected group of azo dyes and the azo dye effects on C. perfringens growth under different media conditions.…”

Section: Discussionmentioning

confidence: 99%

“…Various strains of C. perfringens are known and they differ in the specific type of toxin(s) produced (Ahmad et al, 2010). C. perfringens contains many metabolic capabilities, one of which is azoreductase activity (Morrison et al, 2012(Morrison et al, , 2014Morrison & John, 2013, 2015.…”

Section: Introductionmentioning

confidence: 99%

“…The azoreductase of C. perfringens strain ATCC 3626, AzoC, has been studied previously both biochemically and structurally (Morrison et al, 2012(Morrison et al, , 2014Morrison & John, 2013, 2015. What is lacking from the studies, though, is a look at physiology in terms of the effect of the azo dyes on C. perfringens, as well as the effect of C. perfringens on azo dyes (with and without AzoC).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Growth and physiology of Clostridium perfringens wild-type and ΔazoC knockout: an azo dye exposure study

Morrison

John

2016

Microbiology

Self Cite

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Clostridium perfringens, a strictly anaerobic micro-organism and inhabitant of the human intestine, has been shown to produce the azoreductase enzyme AzoC, an NAD(P)H-dependent flavin oxidoreductase. This enzyme reduces azo dyes to aromatic amines, which are carcinogenic in nature. A significant amount of work has been completed that focuses on the activity of this enzyme; however, few studies have been completed that focus on the physiology of azo dye reduction. Dye reduction studies coupled with C. perfringens growth studies in the presence of ten different azo dyes and in media of varying complexities were completed to compare the growth rates and dye-reducing activity of C. perfringens WT cells, a C. perfringens DazoC knockout, and Bifidobacterium infantis, a non-azoreductase-producing control bacterium. The presence of azo dyes significantly increased the generation time of C. perfringens in rich medium, an effect that was not seen in minimal medium. In addition, azo dye reduction studies with the DazoC knockout suggested the presence of additional functional azoreductases in this medically important bacterium. Overall, this study addresses a major gap in the literature by providing the first look, to our knowledge, at the complex physiology of C. perfringens upon azo dye exposure and the effect that both azo dyes and the azoreductase enzyme have on growth.

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“…It conclusively demonstrating that under aerobic conditions the nitro aromatic compounds were converted efficiently into their corresponding amines by purified flavin-free NADH-azoreductase (Table 3 and Figure 3). Based on properties, the enzymes of monomeric flavin free azoreductases seem to have a different origin but have same chemical function of azo and nitro reduction, suggesting convergent evolution [30]. This flavin-free NADH azoreductase from B. badius contributes to nitro aromatic and azo dye degradation.…”

Section: Analysis Of Transformed Productsmentioning

confidence: 99%

Biotransformation of Nitro Aromatic Compounds by Flavin-Free NADHAzoreductase

Misal¹

2015

J Bioremed Biodeg

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Nitro aromatic compounds are the potential toxic organic pollutant released into the environment and are often resistant to degradation under normal environmental conditions. The biotransformation and/or detoxification of these compounds can be possible by microbial azoreductase enzyme. Azoreductase enzyme has an ability to reduce the toxic nitro group to corresponding amino group. In present report, the flavin-free NADH azoreductase was isolated and purified from alkaliphilic bacteria Bacillus badius. The enzyme was purified by a combination of ammonium sulphate precipitation and size exclusion chromatography. The purified azoreductase has efficiently demonstrated both azoreductase and nitroreductase activities. The biochemical properties of the azoreductase including cofactor requirement, substrate specificity and enzyme inhibition have been studied. The biotransformation of some selected nitro aromatic compounds like 3-nitro benzoic acid, 4-nitro toluene, 3-nitro toluene and 1-chloro-2-nitro benzene by purified azoreductase was carried out at 37°C. The reduction products of these nitro aromatic compounds were analyzed by IR and NMR spectroscopy.

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Identification, Isolation and characterization of a novel azoreductase from Clostridium perfringens

Cited by 58 publications

References 18 publications

Bacterial diversity and composition in major fresh produce growing soils affected by physiochemical properties and geographic locations

Bacterial diversity and composition in major fresh produce growing soils affected by physiochemical properties and geographic locations

Growth and physiology of Clostridium perfringens wild-type and ΔazoC knockout: an azo dye exposure study

Biotransformation of Nitro Aromatic Compounds by Flavin-Free NADHAzoreductase

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