ISSN: 0973-7510

E-ISSN: 2581-690X

Review Article | Open Access
Sonal Chaudhary, Ayushi Singh, Ajit Varma and Shalini Porwal
Amity Institute of Microbial Technology, Amity University, Sector-125, Noida – 201313, Uttar Pradesh, India.
Article Number: 7694 | © The Author(s). 2022
J Pure Appl Microbiol. 2022;16(3):1479-1491. https://doi.org/10.22207/JPAM.16.3.72
Received: 24 March 2022 | Accepted: 04 July 2022 | Published online: 30 August 2022
Issue online: September 2022
Abstract

Biotechnological and industrial processes involve applications of various microorganisms and enzymes, and laccase, as a multifunctional enzyme, is admired for its role in degrading a variety of substances. Laccase is a copper-containing oxidase enzyme that is usually found in insects, plants, and microorganisms including fungi and archaea. Several phenolic substrates are oxidized by laccases, which results in crosslinking. Various research work and industrial solutions have identified the true potential of laccases to degrade various aromatic polymers, and their plausible application in bioremediation and other industries is entirely conceivable. This review focuses on laccases as a multifunctional enzyme and provides an overview of its natural origin, catalytic mechanism, and various methods of production. Further, we discuss the various applications of laccase in the biotechnological arena. We observed that laccase can degrade and detoxify various synthetic compounds. The broad substrate specificity of the same makes it worthy for different fields of industrial applications such as food and bioremediation technology, textile and paper technology, biosensors and nanobiotechnology, biofuel, and various other applications, which are described in this paper. These recent developments in the application of laccase show the multifunctional role of laccase in industrial biotechnology and provide an outlook of laccase as a multifunctional enzyme at the forefront of biotechnology.

Keywords

Laccase, Enzyme, Multifunctional, Biotechnology, Oxidation

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