Synthetic dyes decolorization potential of agroindustrial waste-derived thermo-active laccase from Aspergillus species

Omeje, Kingsley O.; Nnolim, Nonso E.; Ezema, Benjamin E.; Ozioko, Juliet N.; Eze, Sabinus Oscar Onyebuchi

doi:10.1016/j.bcab.2020.101800

Cited by 22 publications

(9 citation statements)

References 30 publications

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“…For fungal cultures, a wide variety of lignocellulosic biomass has been used as an alternative substrate in submerged fermentation, solid-state fermentation or semisolid-state fermentation. Peanut shell, wheat straw, wheat bran, rice straw, rice bran, agave bagasse, sugarcane vinasse, corn bran, fruit peel, tea, sunflower seeds and apple pomace are some of the studied lignocellulosic wastes for Lac production for water remediation [ 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 ].…”

Section: Enzymatic Biodegradationmentioning

confidence: 99%

Current Challenges for Biological Treatment of Pharmaceutical-Based Contaminants with Oxidoreductase Enzymes: Immobilization Processes, Real Aqueous Matrices and Hybrid Techniques

et al. 2022

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The worldwide access to pharmaceuticals and their continuous release into the environment have raised a serious global concern. Pharmaceuticals remain active even at low concentrations, therefore their occurrence in waterbodies may lead to successive deterioration of water quality with adverse impacts on the ecosystem and human health. To address this challenge, there is currently an evolving trend toward the search for effective methods to ensure efficient purification of both drinking water and wastewater. Biocatalytic transformation of pharmaceuticals using oxidoreductase enzymes, such as peroxidase and laccase, is a promising environmentally friendly solution for water treatment, where fungal species have been used as preferred producers due to their ligninolytic enzymatic systems. Enzyme-catalyzed degradation can transform micropollutants into more bioavailable or even innocuous products. Enzyme immobilization on a carrier generally increases its stability and catalytic performance, allowing its reuse, being a promising approach to ensure applicability to an industrial scale process. Moreover, coupling biocatalytic processes to other treatment technologies have been revealed to be an effective approach to achieve the complete removal of pharmaceuticals. This review updates the state-of-the-art of the application of oxidoreductases enzymes, namely laccase, to degrade pharmaceuticals from spiked water and real wastewater. Moreover, the advances concerning the techniques used for enzyme immobilization, the operation in bioreactors, the use of redox mediators, the application of hybrid techniques, as well as the discussion of transformation mechanisms and ending toxicity, are addressed.

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Section: Enzymatic Biodegradationmentioning

confidence: 99%

Current Challenges for Biological Treatment of Pharmaceutical-Based Contaminants with Oxidoreductase Enzymes: Immobilization Processes, Real Aqueous Matrices and Hybrid Techniques

et al. 2022

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“…The effect of pH on laccase activity was investigated using 0.1 mM buffer concentrations of sodium acetate (pH 3.0-5.0), sodium phosphate (pH 6.0-7.0) and Tris-HCl (pH 8.0-9.0). Similarly, the effect of assay temperature on laccase activity was investigated by conducting laccase activity experiments at temperatures ranging from 30 to 70°C (Omeje et al, 2020).…”

Section: Effect Of Ph and Temperature On Laccase Activitymentioning

confidence: 99%

Laccase production from Bacillus aestuarii KSK using Borassus flabellifer empty fruit bunch waste as a substrate and assessing their malachite green dye degradation

Selvam¹,

Ameen

Amirul

et al. 2022

Journal of Applied Microbiology

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Aims:The lignocellulosic waste, Borassus flabellifer empty fruit bunch waste (BFEFBW), was employed to produce laccase using Bacillus aestuarii KSK under solid-state fermentation (SSF) conditions and to assess the efficiency of malachite green (MG) dye decolourization. Methods and Results: Abiotic factors such as pH (5.0-9.0), temperature (25-45°C) and incubation time (24-96 h) were optimized using Response surface methodology-Box-Behenan Design (RSM-BBD) to exploit the laccase production. The anticipated model revealed that the highest laccase activity of 437 U/ml shows after 60 h of incubation at 35°C at pH 7.0. The bacterial laccase was used to remove 89% of the MG dye in less time. Conclusion:The laccase from B. aestuarii KSK decolorizes the MG and thereby making it a suitable choice for wastewater treatment from industrial effluents. Significance and Impact of the Study:This study is the first report on the production of laccase from B. flabellifer empty fruit bunch waste as a substrate. Bacillus aestuarii KSK was isolated from the soil sample and used to produce laccase under SSF conditions. The bacterial laccase has the potential for industrial application in textile waste dye treatment.

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“…It also maintained 90% of its preliminary potential to deteriorate BPA (Brugnari, 2018). The purified laccase from Aspergillus species is reported to decolorize synthetic dyes ranging from 36% for Basic Violet 2 to 83% for Vat Blue 5, indicating that fungal laccases have considerable potential for bioremediation purposes [67].…”

Section: Temperature (ºC)mentioning

confidence: 99%

Fabrication and Catalytic Characterization of Laccase-Loaded Calcium-Alginate Beads for Enhanced Degradation of Dye-Contaminated Aqueous Solutions

et al. 2021

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Engineered laccases represent an eco-friendlier and robust biocatalytic tool for the treatment of dye-harboring textile wastewater. This study investigates the immobilization of purified laccase from Pleurotus sapidus onto firm-quality spherical Caalginate beads by a cross-linking approach. Sodium alginate at an optimal concentration of 4% (w/v) furnished the highest immobilization efficiency (69%). EDX analysis confirmed the detection of copper in the laccase-incorporated alginate beads. The optimum pH for free laccase was 3.0, while the Ca-alginate-Lac showed the maximum enzyme activity (440.2 U/mL) at pH 5.0. In contrast to a free enzyme (40 °C), immobilized laccase performed best at an elevated temperature of 65 °C. The Km and V max values in the case of free and Ca-alginate immobilized enzymes were 114 µM, 370 U/mL, and 123 µM, 548 U/ mL, respectively. Immobilized laccase catalyzed a highly efficient decolorization of various reactive and disperse dye pollutants and recorded in the range of 86.19-91.01%. The COD and TOC levels were substantially reduced to 91.90-94.94 and 77.01-93.29%, respectively, in the maximally degraded dye solutions. Therefore, immobilization of laccase on Ca-alginate beads offers a cost-effective and facile method for environmental remediation applications.

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Synthetic dyes decolorization potential of agroindustrial waste-derived thermo-active laccase from Aspergillus species

Cited by 22 publications

References 30 publications

Current Challenges for Biological Treatment of Pharmaceutical-Based Contaminants with Oxidoreductase Enzymes: Immobilization Processes, Real Aqueous Matrices and Hybrid Techniques

Current Challenges for Biological Treatment of Pharmaceutical-Based Contaminants with Oxidoreductase Enzymes: Immobilization Processes, Real Aqueous Matrices and Hybrid Techniques

Laccase production from Bacillus aestuarii KSK using Borassus flabellifer empty fruit bunch waste as a substrate and assessing their malachite green dye degradation

Fabrication and Catalytic Characterization of Laccase-Loaded Calcium-Alginate Beads for Enhanced Degradation of Dye-Contaminated Aqueous Solutions

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