The rapid growth of the human population in recent decades has resulted in the intensive development of various industries, the development of urban agglomerations and increased production of medicines for animals and humans, plant protection products and fertilizers on an unprecedented scale. Intensive agriculture, expanding urban areas and newly established industrial plants release huge amounts of pollutants into the environment, which, in nature, are very slowly degraded or not decomposed, which leads to their accumulation in water and terrestrial ecosystems. Researchers are scouring extremely contaminated environments to identify organisms that have the ability to degrade resistant xenobiotics, such as PAHs, some pharmaceuticals, plasticizers and dyes. These organisms are a potential source of enzymes that could be used in the bioremediation of industrial and municipal wastewater. Great hopes are pinned on oxidoreductases, including laccase, called by some a green biocatalyst because the end product of the oxidation of a wide range of substrates by this enzyme is water and other compounds, most often including dimers, trimers and polymers. Laccase immobilization techniques and their use in systems together with adsorption or separation have found application in the enzymatic bioremediation of wastewater.

Some Basidiomycota were chosen for studies of key ligninases synthesis (25°C, 30 days) in modified medium (shaken or not cultures) with added wheat straw. Liquid Czapek medium with straw yielded a higher amount of laccase than peroxidase, ground straw induced enzyme worse than chopped straw. With peroxidase the reverse dependencies were observed. Laccase of Lentinus edodes synthesized two enzyme isoforms (ca 30 and 16 kDa). In T. versicolor culture active laccase protein with highest molecular mass ca 65 kDa was found. P. sajor-caju yielded three different peroxidase isoforms. Ligninase biosynthesis depended on strain, straw fragmentation extent, culture method and growth medium.

Environmental pollution with organic substances has become one of the world’s major problems. Although pollutants occur in the environment at concentrations ranging from nanograms to micrograms per liter, they can have a detrimental effect on species inhabiting aquatic environments. Endocrine disrupting compounds (EDCs) are a particularly dangerous group because they have estrogenic activity. Among EDCs, the alkylphenols commonly used in households deserve attention, from where they go to sewage treatment plants, and then to water reservoirs. New methods of wastewater treatment and removal of high concentrations of xenoestrogens from the aquatic environment are still being searched for. One promising approach is bioremediation, which uses living organisms such as fungi, bacteria, and plants to produce enzymes capable of breaking down organic pollutants. These enzymes include laccase, produced by white rot fungi. The ability of laccase to directly oxidize phenols and other aromatic compounds has become the focus of attention of researchers from around the world. Recent studies show the enormous potential of laccase application in processes such as detoxification and biodegradation of pollutants in natural and industrial wastes.

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This review focuses on the enzymatic breakdown of chitin, taking into account the latest scientific reports on the activity of lytic polysaccharide monooxygenase (LPMO). Chitin is a natural, abundant polysaccharide of great practical importance in the environment. However, the insolubility in water and the tightly packed crystalline structure of chitin pose a serious obstacle to enzymatic degradation. This substrate can be converted into soluble sugars by the action of glycosidic hydrolases (GH), also known as chitinases. LPMO could prove to be helpful in enzymatic processes that increase the rate of chitin depolymerisation by improving the availability of substrates for chitinases. The unique action of LPMO is based on the ability to catalyse the oxidative cleavage of glycosidic chains present in complex, resistant crystal networks of chitin, and this cleavage facilitates the subsequent action of glycolytic hydrolases.