Glucose oxidase effect on treatment of textile effluent containing reactive azo dyes by<i>Phanerochaete chrysosporium</i>

Ansari, Zahra; Karimi, Afzal; Sedghi, Shahram; Razzaghi, Mohammad; Ebrahimi, Sirous

doi:10.1002/jctb.5170

Cited by 12 publications

(5 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Degradation of mycotoxins in oxalate and citrate is of physiological relevance since, in nature, the fungi expressing MnPs can also produce these two compounds in their cellular metabolism [ 22 ]. Additionally, it has been reported that gluconic acid, cellobionic acid, and other organic acids as well, can aid manganese peroxidases to exert their degradation on lignin molecules [ 31 ]. This allows the fungi to use manganese peroxidases, in assistance with these naturally occurring molecules, to break the lignin barrier apart and capture energy from the plant cell wall polysaccharides [ 32 ].…”

Section: Resultsmentioning

confidence: 99%

Patulin Detoxification by Recombinant Manganese Peroxidase from Moniliophthora roreri Expressed by Pichia pastoris

Wang

Penttinen

et al. 2022

Toxins

View full text Add to dashboard Cite

The fungal secondary metabolite patulin is a mycotoxin widespread in foods and beverages which poses a serious threat to human health. However, no enzyme was known to be able to degrade this mycotoxin. For the first time, we discovered that a manganese peroxidase (MrMnP) from Moniliophthora roreri can efficiently degrade patulin. The MrMnP gene was cloned into pPICZα(A) and then the recombinant plasmid was transformed into Pichia pastoris X-33. The recombinant strain produced extracellular manganese peroxidase with an activity of up to 3659.5 U/L. The manganese peroxidase MrMnP was able to rapidly degrade patulin, with hydroascladiol appearing as a main degradation product. Five mg/L of pure patulin were completely degraded within 5 h. Moreover, up to 95% of the toxin was eliminated in a simulated patulin-contaminated apple juice after 24 h. Using Escherichia coli as a model, it was demonstrated that the deconstruction of patulin led to detoxification. Collectively, these traits make MrMnP an intriguing candidate useful in enzymatic detoxification of patulin in foods and beverages.

show abstract

Section: Resultsmentioning

confidence: 99%

Patulin Detoxification by Recombinant Manganese Peroxidase from Moniliophthora roreri Expressed by Pichia pastoris

Wang

Penttinen

et al. 2022

Toxins

View full text Add to dashboard Cite

show abstract

“…5B) because the activity of MnP in the P system after 3 h treatment was higher than the initial amount. The effect of active pyranose 2-oxidase on MnP is same as MnP with glucose oxidase (Ansari et al 2016(Ansari et al , 2017. In the C system, LiP and MnP of 3 h treatment was 0.021 IU/mL and 0.75 IU/mL.…”

Section: Residual Enzyme Activities After Pyranose 2-oxidase Lignin-dmentioning

confidence: 86%

Synergetic depolymerization of aspen CEL by pyranose 2-oxidase and lignin-degrading peroxidases

Wang

Huang

2019

BioRes

View full text Add to dashboard Cite

Three enzymatic treatments were compared for the depolymerization of cellulolytic enzyme lignin (CEL) from aspen; these systems used pyranose 2-oxidase and lignin-degrading peroxidases. The “P” system was mainly composed of pyranose 2-oxidase, lignin peroxidase (LiP), and manganese peroxidase (MnP). Catalase and vitamin C were added to the P system to decompose H2O2 to control the H2O2 concentration. The system to which catalase was added was called the “C” system. The system to which catalase and vitamin C were added together was called the “V” system. Ultraviolet-visible (UV-Vis) spectra of supernatants after aspen CEL treatment by the P, C, or V system was used to monitor the amount of water-soluble lignin fragments that were generated, which increased with system treatment time. A gel permeation chromatography (GPC) analysis showed that after 12 h of system treatment, the molecular weight (Mw) of CEL was efficiently lowered; the maximum Mw reduction of aspen CEL was 20% when compared to the blank and control runs. The residual enzymatic activity of the supernatant after the CEL treatment by the P, C, or V system indicated that MnP and LiP activity for lignin degradation was dependent upon the H2O2 concentration. Therefore, it is advised that MnP and LiP be applied separately for effective lignin degradation.

show abstract

“…[90][91][92][93][94][95][96] One study found that MnP of P. Chrysosporium was the main enzyme involved in the discoloration of textile dyes. 97 This crude or purified enzyme's potential has also been reported, mainly to discolor various types of synthetic dyes. 93 In the study directed by Zhang et al, 85 MnP crude and purified from the fungus Cerrena unicolor BBP6 was used in the discoloration of solutions of Congo red dyes, MO, Remazol bright blue R, bromophenol blue, and crystal violet.…”

Section: Manganese Peroxidasementioning

confidence: 97%

Oxidoreductases as a versatile biocatalytic tool to tackle pollutants for clean environment – a review

Bilal

Bagheri

Vilar

et al. 2021

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

With the growing population and rapid industrial development of the world, various pollutantsexplicitly known as emerging pollutants (EPs) and including micro and nanoplastics, pharmaceuticals, hazardous dyes, steroid estrogen, and organic pollutantscontinue to enter into the environment and water sources. These EPs cause a variety of side effects and diseases, such as cancer, neurotoxic and mutagenic effects, stomach cramps, intestinal disorders, loss of peripheral vision, deteriorated movement coordination, and weakened muscles, even in low concentrations. The presence of EPs in the environment/water sources affects humans and animals and disturbs ecological integrity. Therefore, removing these EPs from the environment with a smart, greener, and environmentally competent technology has become a meaningful goal. Most of the EPs are stable in the media, and their removal is a considerable scientific challenge. Different treatment methods, like adsorption and degradation processes, have been used to eliminate these pollutants. Enzyme-mediated approaches hold immense prospects in environmental cleanup and have been keenly explored recently. Many efforts have been made to apply biocatalytic-based materials, like laccases and peroxidases, as unique tools alongside a powerful oxidation approach for the degradation and treatment of EPs. These enzymes' unique properties in terms of excellent selectivity and exclusive catalytic features make them robust candidates for biocatalytic treatment. This work spotlights the biocatalytic properties and application of oxidoreductases to remove EPs. The challenges, conclusive remarks, and standpoints for robust biocatalysts are also given.

show abstract

Glucose oxidase effect on treatment of textile effluent containing reactive azo dyes byPhanerochaete chrysosporium

Cited by 12 publications

References 39 publications

Patulin Detoxification by Recombinant Manganese Peroxidase from Moniliophthora roreri Expressed by Pichia pastoris

Patulin Detoxification by Recombinant Manganese Peroxidase from Moniliophthora roreri Expressed by Pichia pastoris

Synergetic depolymerization of aspen CEL by pyranose 2-oxidase and lignin-degrading peroxidases

Oxidoreductases as a versatile biocatalytic tool to tackle pollutants for clean environment – a review

Contact Info

Product

Resources

About