Fungal Laccase: A Versatile Enzyme for Biotechnological Applications

Rodríguez‐Couto, Susana

doi:10.1007/978-3-030-10480-1_13

Cited by 26 publications

(14 citation statements)

References 116 publications

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“…There are more than 15 laccase-based commercial products used in the textile, food and paper industry, which reflects the viability of their industrial use [199]. The most successful and versatile applications have been developed for the textile industry, particularly for the bleaching of indigo-stained denim, such as Denilitel, DeniliteITM, Zylite, and Bleach-cut 3S.…”

Section: Potential Application Of Laccases In Water Bioremediationmentioning

confidence: 99%

“…The most successful and versatile applications have been developed for the textile industry, particularly for the bleaching of indigo-stained denim, such as Denilitel, DeniliteITM, Zylite, and Bleach-cut 3S. Furthermore, the commercialization of the laccase Metzyme, which has high ligninolytic properties, opens the possibility of commercial use of other laccases in the near future [199]. Unfortunately, no commercial laccase products for water treatment are available yet.…”

Section: Potential Application Of Laccases In Water Bioremediationmentioning

confidence: 99%

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Laccases: structure, function, and potential application in water bioremediation

et al. 2019

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The global rise in urbanization and industrial activity has led to the production and incorporation of foreign contaminant molecules into ecosystems, distorting them and impacting human and animal health. Physical, chemical, and biological strategies have been adopted to eliminate these contaminants from water bodies under anthropogenic stress. Biotechnological processes involving microorganisms and enzymes have been used for this purpose; specifically, laccases, which are broad spectrum biocatalysts, have been used to degrade several compounds, such as those that can be found in the effluents from industries and hospitals. Laccases have shown high potential in the biotransformation of diverse pollutants using crude enzyme extracts or free enzymes. However, their application in bioremediation and water treatment at a large scale is limited by the complex composition and high salt concentration and pH values of contaminated media that affect protein stability, recovery and recycling. These issues are also associated with operational problems and the necessity of large-scale production of laccase. Hence, more knowledge on the molecular characteristics of water bodies is required to identify and develop new laccases that can be used under complex conditions and to develop novel strategies and processes to achieve their efficient application in treating contaminated water. Recently, stability, efficiency, separation and reuse issues have been overcome by the immobilization of enzymes and development of novel biocatalytic materials. This review provides recent information on laccases from different sources, their structures and biochemical properties, mechanisms of action, and application in the bioremediation and biotransformation of contaminant molecules in water. Moreover, we discuss a series of improvements that have been attempted for better organic solvent tolerance, thermo-tolerance, and operational stability of laccases, as per process requirements.

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Section: Potential Application Of Laccases In Water Bioremediationmentioning

confidence: 99%

Section: Potential Application Of Laccases In Water Bioremediationmentioning

confidence: 99%

Laccases: structure, function, and potential application in water bioremediation

et al. 2019

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“…Type II and III together forms the trinuclear cluster of laccases where dioxygen binds and four electron reduction to water takes place. It is due these features that laccase has its application in wide range of industries [4] e.g., clarification of beverage, paper and pulp, textile industry, biosensor, bioremediation and organic synthesis [51]. However, the catalytic ability of enzymes is often hindered in harsh environments like high-acid and high-alkaline solutions due to transformations of enzyme structure which results in low operational stability, difficulties in recovery and reuse [5].…”

Section: Introductionmentioning

confidence: 99%

Multicopper oxidase laccases with distinguished spectral properties: A new outlook

Agrawal

Verma

2020

Heliyon

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Multicopper oxidases (MCOs) has a unique feature of having the presence of four Cu atoms arranged into three (Type I, II and III) spectral classification. MCOs laccase due to its broad range of substrate specificity has numerous biotechnological applications. The two types of laccases include the typical blue and the atypical white, yellow laccases which have been isolated from diverse geographical locations globally. In the present study laccases were identified using Liquid Chromatograph Mass Spectrometer Studies (LCMS) study where blue laccase exhibited homology with Trametes villosa Q99044 and Q99046 and white, yellow laccase exhibited homology with Myrothecium verrucaria OX ¼ 1859699; Q12737 and Trametes versicolor Q12717 respectively. The spectral comparison between laccases were determined via spectroscopic analysis where UV-spectra of blue laccase from Trametes versicolor had a peak at 605 nm (Type I Cu atom) whereas in case of white and yellow laccases the peak was absent and in addition had an absorption peak at 400nm. It was followed by X-Ray Diffraction (XRD) analysis of proteins where α-helix (10 ) and β-sheet (22 ) structure were observed in case of all the three laccases. However, the intensity of α-helix in white and yellow laccase was stronger as compared to the blue laccase whereas the intensity of β-sheet was stronger in case of blue laccase as compared to other two laccases. Further, Fourier-transform infrared spectroscopy (FTIR) analysis was performed which enabled the analysis of proteins where α-helix (1650-1658 cm À1 ), β-sheets (1620-1640 cm À1 ), amide I (1700À1600 cm À1 ) amide II (bands at under 1400 cm À1 ) and amide A, B (bands above 3000 cm À1 ).

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“…Of these, white-rot fungi and other litter degrading organisms are the most prominent sources of the laccase enzyme. In specific, laccase production by basidiomycetous taxa such as Trametes, Pleurotus, Agaricus, Phanerochaete, Pycnoporus, and Lentinus has been broadly explored as they are easy to grow in in vitro (Rodríguez-Couto, 2019). White-rot fungal species that synthesize laccase are Polyporus sanguineus, Phlebia brevispora, Daedalea flavida and Phlebia radiata (Arora, Gill 2001), Phanerochaete chrysosporium, Trametes hirsuta, Marasmius sp.…”

Section: Laccasementioning

confidence: 99%

Untitled

2021

EEB

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Xenobiotics are hazardous compounds that are foreign to natural ecosystems. The production and use of xenobiotic compounds continue to increase worldwide, which in turn causes environmental pollution and has adverse effects on humans. Degradation of such compounds, therefore, needs urgent awareness and attention. The physicochemical approaches to treat the contaminants are expensive. Bioremediation is a concept that exploits organisms to manage the environment with less manpower and time. White-rot fungi-mediated bioremediation offers inexpensive, environmentally sustainable and potential degradation mechanisms for different recalcitrant chemicals. White-rot fungi secrete lignolytic enzymes that have extensive substrate specificities and are involved in the transformation and solubilization of lignin-like structural contaminants. The main lignolytic enzymes occurring in white-rot fungi are laccases, lignin peroxidase, manganese peroxidase, and other peroxidases. Such lignolytic enzymes permit white-rot fungi to endure high toxic levels. This review describes the opportunities to use white-rot fungi and their enzyme systems in the biodegradation of multiple xenobiotic contaminants.

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Fungal Laccase: A Versatile Enzyme for Biotechnological Applications

Cited by 26 publications

References 116 publications

Laccases: structure, function, and potential application in water bioremediation

Laccases: structure, function, and potential application in water bioremediation

Multicopper oxidase laccases with distinguished spectral properties: A new outlook

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