About this Research Topic

Background

Laccases (E.C. 1.10.3.2) are considered one of the most important ligninolytic oxidative enzymes, capable of oxidizing phenolic and non-phenolic subunits of lignin model compounds as well as highly recalcitrant environmental pollutants which help researchers to put them in various biotechnological applications. The broad substrate range of laccases that is derived from their non-specific formation of a free radical from a suitable substrate, and the use of air oxygen as a second substrate, make laccases attractive candidates for industrial application. Laccases play an important role in the food industry, paper and pulp industry, textile industry, synthetic chemistry, cosmetics, soil bioremediation and biodegradation of environmental phenolic pollutants, removal of endocrine disruptors, biosensor and analytical applications.
In view of the many applications which can be done by laccase including environmental pollution control, lignocellulose modification, textile industry, biosensors, food industry, pharmaceutical industry, and organic synthesis, it seems likely that laccase will be one of the most important biotechnological catalysts in the foreseeable future.
Many industries are currently pursuing enzymatic approaches for developing green chemistry technologies mainly due to shortcomings of physico-chemical methods, growing environmental concerns, legal restrictions, and increasing scientific knowledge. Laccase-assisted reactions, in particular, are being intensively investigated as they are generally eco-friendly and have wide application potential. Laccases only require oxygen as co-substrate; they release water as the only by-product and have a wide substrate range which can be further extended by the use of laccase–mediator systems. Chemical attachment of reactive anchor groups to unreactive polymers, for subsequent coupling of laccase substrates, has also widened application areas.
Recent efforts to enzyme modification by chemical or biotechnological means may help to improve enzyme activity and stability. So, efforts to improve immobilization techniques also need to be intensified. Although several methods have been developed to immobilize laccase, many have the major drawback of fast deactivation of the enzyme. However, a new immobilization technique has been developed for the production of chemically bonded immobilized laccase with better stability and oxidizing capability than free laccase. Due to their diversified distributions and functions, laccases are looked upon as potential eco-friendly enzymes to replace the conventional chemical and mechanical processes in several industries such as the pulp and paper, textile, pharmaceutical as well as nanoparticle-based biosensor. 
The aim of the current Research Topic is to cover promising, recent, and novel research trends in the microbial laccases field. We welcome original research, mini-reviewes and review articles only. Areas to be covered in this Research Topic may include, but are not limited to:· Maximize the microbial laccases production via the development of advanced proteomic techniques, chemical engineering, and statistical approaches.· Purification, characterization, and applications of microbial laccases with exceptional properties.· Laccase immobilization over various novel supports like nanocomposites for unique applications like: laccase biosensors, laccase biofuel cells, or other advanced possible biotechnological and environmental applications.

Keywords: Microbial laccases, genetic modifications, overproduction, kinetic modelling, applications

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