Immobilized Peroxidase Catalyzed Decolorization and Degradation of Industrially Important Dyes from Polluted Water

Husain, Qayyum

doi:10.1007/978-3-030-25023-2_7

Cited by 3 publications

(2 citation statements)

References 98 publications

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“…Peroxidases are another group of enzymes that can catalyze oxidation reactions. Peroxidases immobilized on various kinds of supports have been successfully utilized for the decolorization and detoxification of waste dyes [23,[58][59][60]. Many researchers have also used horseradish peroxide (HRP) in the degradation of organic dyes.…”

Section: Organic Dyesmentioning

confidence: 99%

“…There have been several reviews on the role of immobilized enzymes in environmental applications, describing various types of biocatalytic systems based on oxidoreductases (laccase and peroxidase) and their use as catalysts in wastewater treatment. Some of them concern immobilized laccases [19, 20•, 21] and peroxidases [22][23][24] and their potential application to remediate pollutants. Others refer to methods of immobilization, the support matrices used, and the types of pollutants treated [8,[25][26][27].…”

Section: Introductionmentioning

confidence: 99%

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Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

Kołodziejczak-Radzimska

Nghiem

Jesionowski

2021

Curr Pollution Rep

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Purpose of Review Untreated wastewater discharge can significantly and negatively impact the state of the environment. Rapid industrialization and economic development have directly contributed to land and water pollution resulting from the application of many chemicals such as organic dyes, pharmaceuticals, and industrial reagents. The removal of these chemicals before effluent discharge is crucial for environmental protection. This review aims to explore the importance of functionalized materials in the preparation of biocatalytic systems and consider their application in eliminating water pollutants. Recent Findings Wastewater treatment methods can be classified into three groups: (i) chemical (e.g., chemical oxidation and ozonation), (ii) physical (e.g., membrane separation and ion exchange), and (iii) biological processes. Biological treatment is the most widely used method due to its cost-effectiveness and eco-friendliness. In particular, the use of immobilized enzymes has recently become more attractive as a result of scientific progress in advanced material synthesis. The selection of an appropriate support plays an important role in the preparation of such biologically active systems. Recent studies have demonstrated the use of various materials for enzyme immobilization in the purification of water. Summary This review identifies and discusses different biocatalytic systems used in the enzymatic degradation of various water pollutants. Materials functionalized by specific groups can serve as good support matrices for enzyme immobilization, providing chemical and thermal stability to support catalytic reactions. Enzymatic biocatalysis converts the pollutants into simpler products, which are usually less toxic than their parents. Due to immobilization, the enzyme can be used over multiple cycles to reduce the cost of wastewater treatment. Future studies in this field should focus on developing new platforms for enzyme immobilization in order to improve degradation efficiency.

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Section: Organic Dyesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

Kołodziejczak-Radzimska

Nghiem

Jesionowski

2021

Curr Pollution Rep

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An accomplished procedure of horseradish peroxidase immobilization for removal of acid yellow 11 in aqueous solutions

Yapaöz

Attar

2020

Water Science and Technology

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Horseradish peroxidase (HRP) characteristics were improved by two techniques, Na-alginate entrapment and glutaraldehyde crosslinking prior to alginate entrapment, in order to enhance the stability, functionality and removal of dyes in waste water. Free, entrapped and crosslinked-entrapped enzymes were compared by activity assays indicated the optimum temperature is 25 °C and pH 4.0–5.0. Kinetics results showed that alginate entrapment and crosslinking prior to entrapment increased Vmax and did not cause any significant decrease in Km. The thermal resistance of the free enzyme was short-term, zero residual activity after 250 min while the immobilized enzymes preserved more than 50% of their activity for 5 h at 60 °C. Immobilized HRP was resistant to methanol, ethanol, DMSO and THF. The storage stability of free HRP ended in 35 days whereas entrapped and crosslinked-entrapped HRPs had 87 and 92% residual activity at 60th day, respectively. HRP was used in the decolorization of azo dye Acid yellow 11 and total decolorization (>99%) was obtained using crosslinked-entrapped HRP. Reusability studies presented the improvement that crosslinked-entrapped HRP reached 74% decolorization after 10 batches. The results demonstrated that the novel immobilized HRP can be used as an effective catalyst for dye degradation of industrial waste effluents.

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Exploring the Diversity of Fungal DyPs in Mangrove Soils to Produce and Characterize Novel Biocatalysts

Ayed

Saint-Genis

Vallon

et al. 2021

JoF

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The functional diversity of the New Caledonian mangrove sediments was examined, observing the distribution of fungal dye-decolorizing peroxidases (DyPs), together with the complete biochemical characterization of the main DyP. Using a functional metabarcoding approach, the diversity of expressed genes encoding fungal DyPs was investigated in surface and deeper sediments, collected beneath either Avicennia marina or Rhizophora stylosa trees, during either the wet or the dry seasons. The highest DyP diversity was observed in surface sediments beneath the R. stylosa area during the wet season, and one particular operational functional unit (OFU1) was detected as the most abundant DyP isoform. This OFU was found in all sediment samples, representing 51–100% of the total DyP-encoding sequences in 70% of the samples. The complete cDNA sequence corresponding to this abundant DyP (OFU 1) was retrieved by gene capture, cloned, and heterologously expressed in Pichia pastoris. The recombinant enzyme, called DyP1, was purified and characterized, leading to the description of its physical–chemical properties, its ability to oxidize diverse phenolic substrates, and its potential to decolorize textile dyes; DyP1 was more active at low pH, though moderately stable over a wide pH range. The enzyme was very stable at temperatures up to 50 °C, retaining 60% activity after 180 min incubation. Its ability to decolorize industrial dyes was also tested on Reactive Blue 19, Acid Black, Disperse Blue 79, and Reactive Black 5. The effect of hydrogen peroxide and sea salt on DyP1 activity was studied and compared to what is reported for previously characterized enzymes from terrestrial and marine-derived fungi.

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Immobilized Peroxidase Catalyzed Decolorization and Degradation of Industrially Important Dyes from Polluted Water

Cited by 3 publications

References 98 publications

Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

An accomplished procedure of horseradish peroxidase immobilization for removal of acid yellow 11 in aqueous solutions

Exploring the Diversity of Fungal DyPs in Mangrove Soils to Produce and Characterize Novel Biocatalysts

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