Editorial: Microbial Laccases: Recent Advances and Biotechnological Applications

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Recent Advances and Biotechnological ApplicationsMany sectors are presently investigating enzymatic techniques for creating green chemistry technologies, owing to the drawbacks of physico-chemical processes, rising environmental concerns, regulatory constraints, and expanding scientific understanding.Laccases (E.C. 1.10.3.2) are regarded as one of the most important ligninolytic oxidative enzymes, capable of oxidizing both phenolic and non-phenolic subunits of lignin model compounds as well as highly recalcitrant environmental pollutants, allowing researchers to use them in a variety of biotechnological applications.Laccases are appealing prospects for industrial use due to their broad substrate range and that they only need environmental molecular oxygen to exert their catalytic action, producing water as the only byproduct.In addition, such broad substrate range can be expanded further in the presence of the so-called redox mediators that are small molecular weight organic compounds acting as electron shuttles between the substrate and laccase.Laccases are used in the environmental pollution control, food industry, the paper and pulp industry, the textile industry, synthetic chemistry, cosmetics, soil bioremediation and biodegradation of environmental phenolic pollutants, removal of endocrine disruptors, biosensor and analytical applications (Leynaud Kieffer Curran et al., 2022).Given the numerous applications that laccases can perform; it appears likely that laccases will be one of the most important biotechnological catalysts in the near future.Laccase-assisted reactions, in particular, are receiving a lot of attention since they are typically eco-friendly and have a lot of application possibilities.Chemically attaching reactive anchor groups to unreactive polymers for subsequent coupling of laccase substrates has broadened application fields as well.Recent chemical or biotechnological approaches to modify enzymes may aid in improving enzyme activity and stability.Numerous strategies for immobilizing laccase have been devised to produce reusable laccase biocatalysts with more stability and oxidizing ability (Daronch et al., 2020;Zhou et al., 2021).Based on this context, this specific Research Topic has been developed to focus on promising, recent, and unique research developments in the field of microbial laccases.This Research Topic has attracted 31 writers who have contributed to publications.As a result, this Research Topic has provided six peer-reviewed papers to fulfill the needs of the readers, comprising five Original Researches and one Review, all of which covered different elements and corners of this field.From the point that enzymatic polymerization of lignin may provide a wide range of added-value products while also substituting fossil-based resources.Mayr et al. employed a laccase from the thermophilic fungus Myceliophthora thermophila (MtL) as a model substrate to connect a hydrophobicity boosting fluorophenol (FP) molecule onto lignosulfonate (LS).Fluorescence,

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