Elucidating the choice for a precise matrix for laccase immobilization: A review

The use of enzymes as biocatalysts for many industrial processes has grown widely. Laccase, a versatile oxidoreductase enzyme, has been used as a catalyst in a multidisciplinary field. This enzyme can be used for clarification in the food industry, in the chemical industry for organic synthesis of pharmaceuticals and dyes, in the treatment of pollutants in the textile industry for dyes discoloration and endocrine disruptor removal. It can also be used in the manufacture of biosensors for phenol detection, among other applications. In general, laccases are capable of oxidizing phenolic compounds and, using low molecular weight compounds as a mediator to increase their redox potential. They are capable of oxidizing non-phenolic compounds as well. To improve the enzyme properties and to enable its reuse, the immobilization of the laccase onto several different types of supports has been done: inorganic, organic (natural or synthetic) and also hybrids. Unlike other biocatalysts, as lipases, which are effectively immobilized and already commercialized, laccase has on its catalytic site copper atoms that make difficult the stabilization of the final biocatalyst. Based on this characteristic of laccases and the need for making possible its application in potential industrial processes, there is a need to find a suitable way to immobilize this enzyme and then enable the commercialization of a stable biocatalyst, resistant to process conditions and with a long shelf life. This review summarizes the most recently used support materials in academic studies. Moreover, the properties of the final biocatalyst and its application are critically discussed. This work intends to provide the foundation to facilitate the choice of support for laccase immobilization in future works.