Fungal laccase in the textile industry

Rodríguez‐Couto, Susana

doi:10.1002/9781118958308.ch5

Cited by 4 publications

(2 citation statements)

References 55 publications

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“…These sequences contain four (L1, L2, L3, L4) contiguous fragments of copper-binding amino acid residues, whose degree of similarity, depending on the organism from which the enzyme is derived, can range from 75 to 85%. The L2 and L4 regions allow the enzyme to be classified as MCO, whereas the L1 and L3 sequences indicate the subgroup of the enzyme [17].…”

Section: Sahaymentioning

confidence: 99%

Multicopper Oxidases Enzymes use and its Characteristics

Sahay¹

2022

IJAERS

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Multicopper oxidases are a large family of blue copper proteins which contain from one to six copper atoms per molecule. Their catalytic centre consists of three domains which involve type-1 Cu, type-2 Cu and a pair of type-3 Cu's. They include laccases, ferroxidases, ascorbate oxidase, bilirubin oxidase, laccase like multicopper oxidases. MCOs are capable of one electron oxidizing of aromatic as well as non-aromatic compounds with a concomitant four-electron reduction of molecular oxygen to water. These properties make them a valuable tool in various industries (food, textile, pharmaceutical) medicine or environment protection.

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Section: Sahaymentioning

confidence: 99%

Multicopper Oxidases Enzymes use and its Characteristics

Sahay¹

2022

IJAERS

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“…The benefits of the application are relevant and include fewer chemicals, energy and water-saving features, thus contributing to a more environmentally friendly process. Laccase is also used in situ to convert dye precursors for better, more efficient fabric dyeing (Rodríguez-Couto 2015 ). The treatment of wastewater polluted with indigo and other dyes has also been investigated using commercial laccases.…”

Section: Scientific Production Current Applications and Patentsmentioning

confidence: 99%

Laccases as green and versatile biocatalysts: from lab to enzyme market—an overview

Brugnari

Braga

Santos

et al. 2021

Bioresour. Bioprocess.

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Laccases are multi-copper oxidase enzymes that catalyze the oxidation of different compounds (phenolics and non-phenolics). The scientific literature on laccases is quite extensive, including many basic and applied research about the structure, functions, mechanism of action and a variety of biotechnological applications of these versatile enzymes. Laccases can be used in various industries/sectors, from the environmental field to the cosmetics industry, including food processing and the textile industry (dyes biodegradation and synthesis). Known as eco-friendly or green enzymes, the application of laccases in biocatalytic processes represents a promising sustainable alternative to conventional methods. Due to the advantages granted by enzyme immobilization, publications on immobilized laccases increased substantially in recent years. Many patents related to the use of laccases are available, however, the real industrial or environmental use of laccases is still challenged by cost–benefit, especially concerning the feasibility of producing this enzyme on a large scale. Although this is a compelling point and the enzyme market is heated, articles on the production and application of laccases usually neglect the economic assessment of the processes. In this review, we present a description of laccases structure and mechanisms of action including the different sources (fungi, bacteria, and plants) for laccases production and tools for laccases evolution and prediction of potential substrates. In addition, we both compare approaches for scaling-up processes with an emphasis on cost reduction and productivity and critically review several immobilization methods for laccases. Following the critical view on production and immobilization, we provide a set of applications for free and immobilized laccases based on articles published within the last five years and patents which may guide future strategies for laccase use and commercialization.

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Decolorization of Rhodamine B and conversion into saturated fatty acids by laccase-producing fungi isolated from lake sediment

Thipraksa,

Michu,

Kongthong

et al. 2024

J. Degrade. Min. Land Manage.

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The persistence of the carcinogenic Rhodamine B dye poses significant risks to human health. Utilizing a unique fungal strain for its degradation offers a sustainable solution to mitigate these hazards. Bioremediation techniques have demonstrated substantial promise in addressing recalcitrant pollutants such as dyes. In this particular study, laccase-producing fungi were carefully chosen for their potential to break down the toxic textile dye Rhodamine B. These selected fungi Cerrena unicolor FBR03 exhibited an impressive maximum degradation rate of 95.10%. Additionally, an analysis using GC-MS revealed the emergence of breakdown products, including 2-cyclopenten-1-one, 3-hydroxy-2-methyl, thymine, dodecanoic acid, tetradecanoic acid, n-hexadecanoic acid, and dibutyl phthalate. These results underscore the potential of this fungal strain as a promising organism for the effective degradation of dye compounds, while simultaneously producing valuable saturated fatty acids as by-products.

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Fungal laccase in the textile industry

Cited by 4 publications

References 55 publications

Multicopper Oxidases Enzymes use and its Characteristics

Multicopper Oxidases Enzymes use and its Characteristics

Laccases as green and versatile biocatalysts: from lab to enzyme market—an overview

Decolorization of Rhodamine B and conversion into saturated fatty acids by laccase-producing fungi isolated from lake sediment

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