Abstract
Laccase belongs to a small group of enzymes called the blue multicopper oxidases, having the potential ability of oxidation. It belongs to enzymes, which have innate properties of reactive radical production, but its utilization in many fields has been ignored because of its unavailability in the commercial field. There are diverse sources of laccase producing organisms like bacteria, fungi and plants. In fungi, laccase is present in Ascomycetes, Deuteromycetes, Basidiomycetes and is particularly abundant in many white-rot fungi that degrade lignin. Laccases can degrade both phenolic and non-phenolic compounds. They also have the ability to detoxify a range of environmental pollutants. Due to their property to detoxify a range of pollutants, they have been used for several purposes in many industries including paper, pulp, textile and petrochemical industries. Some other application of laccase includes in food processing industry, medical and health care. Recently, laccase has found applications in other fields such as in the design of biosensors and nanotechnology. The present review provides an overview of biological functions of laccase, its mechanism of action, laccase mediator system, and various biotechnological applications of laccase obtained from endophytic fungi.
Highlights
Laccase is one of the few enzymes that have been the subject of study since the end of the last century
The present review provides an overview of biological functions of laccase, its mechanism of action, laccase mediator system, and various biotechnological applications of laccase obtained from endophytic fungi
Compounds which are structurally similar to lignin can be oxidized (Thurston 1994) by fungal laccase along with ferroxidases (EC 1.16.3.1) and ascorbate oxidase (EC 1.10.3.3) from the family of extranuclear multicopper oxidases (MCOs), which in turn belong to the highly diverse group of blue copper proteins
Summary
Laccase is one of the few enzymes that have been the subject of study since the end of the last century. In 1883, laccase was first described by Yoshida when he extracted it from the exudates of the Japanese lacquer tree, Rhus vernicifera (Yoshida 1883). Their characteristic as a metal containing oxidase was discovered by Bertrand (1985). MCOs typically contain two or four copper atoms per protein molecule and they catalyze oxidation reactions In these reactions, electrons are removed from the reducing substrate molecules and transferred to oxygen in order to form water without the step of hydrogen peroxide formation (Ducros et al 1998). The simple requirements of laccase catalysis (presence of substrate and O2), as well as its apparent stability and lack of inhibition (as has been observed with H2O2 for peroxidase), make this enzyme both suitable and attractive for industrial applications. Laccase can oxidize a wide range of organic and inorganic substrates, including mono, di, polyphenols, aminophenols, methoxyphenols as well as metal complexes which are the major reason for their attractiveness for dozens of biotechnological applications
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