Abstract

Laccases are blue multicopper oxidases, which catalyze the monoelectronic oxidation of a broad spectrum of substrates, for example, ortho- and para-diphenols, polyphenols, aminophenols, and aromatic or aliphatic amines, coupled with a full, four-electron reduction of O2 to H2O. Hence, they are capable of degrading lignin and are present abundantly in many white-rot fungi. Laccases decolorize and detoxify the industrial effluents and help in wastewater treatment. They act on both phenolic and nonphenolic lignin-related compounds as well as highly recalcitrant environmental pollutants, and they can be effectively used in paper and pulp industries, textile industries, xenobiotic degradation, and bioremediation and act as biosensors. Recently, laccase has been applied to nanobiotechnology, which is an increasing research field, and catalyzes electron transfer reactions without additional cofactors. Several techniques have been developed for the immobilization of biomolecule such as micropatterning, self-assembled monolayer, and layer-by-layer techniques, which immobilize laccase and preserve their enzymatic activity. In this review, we describe the fungal source of laccases and their application in environment protection.

Highlights

  • Fungi can exploit marginal living conditions in large part because they produce unusual enzymes capable of performing chemically difficult reactions [1, 2]

  • Recent studies have suggested that lignin-degrading or white-rot fungi such as Phanerochaete chrysosporium and Trametes versicolor could replace some of the chemical steps used in paper making [2, 7]

  • The use of enzymes for the treatment or the removal of environmental and industrial pollutants has attracted increasing attention because of their high efficiency, high selectivity, and environmentally benign reactions. Of these enzymes studied for such purposes extracellular fungal peroxidases, such as lignin peroxidase, manganese peroxidase, and fungal laccases are the two major classes of enzymes that have been evaluated for the removal of toxic phenolic compounds from industrial wastewater and the degradation of recalcitrant xenobiotics

Read more

Summary

Introduction

Fungi can exploit marginal living conditions in large part because they produce unusual enzymes capable of performing chemically difficult reactions [1, 2]. Interest in laccases has increased recently because of their potential use in the detoxification of pollutants and in bioremediation of phenolic compounds [3,4,5] These fungal enzymes can convert wood, plastic, paint, and jet fuel among other materials into nutrients. The use of enzymes for the treatment or the removal of environmental and industrial pollutants has attracted increasing attention because of their high efficiency, high selectivity, and environmentally benign reactions Of these enzymes studied for such purposes extracellular fungal peroxidases, such as lignin peroxidase, manganese peroxidase, and fungal laccases are the two major classes of enzymes that have been evaluated for the removal of toxic phenolic compounds from industrial wastewater and the degradation of recalcitrant xenobiotics. The current status of knowledge with regard to fungal laccase and their applications to protect environment is reviewed

Distribution and Physiological Functions of Laccases
Screening of Fungal Species
Cultural and Nutritional Conditions for Laccase Production
Laccases Inducers
Purification and Biochemical Properties of Laccases
Molecular Biology of Laccases
Mode of Action
Biotechnological Applications of Laccase
10. Laccases Role in Bioremediation
10.4. Laccases
10.5. Laccases
Findings
11. Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call