School of Technology and Management, Polytechnic Institute of Leiria, Morro do Lena-Alto do Vieiro, 2411-901 Leiria, Portugal.
UCIBIO-NOVA University of Lisbon, Lisbon, Portugal.
Curr Protein Pept Sci. 2022;23(6):402-423. doi: 10.2174/1389203723666220704090416.
Laccases and peroxidases have attracted great interest for industrial and environmental applications. These enzymes have a broad substrate range and a robust oxidizing ability. Moreover, using mediators or co-oxidants makes it possible to increase their catalytic activity and extend their substrate scope to more resistant chemical structures.
Fungal laccases and ligninolytic peroxidases, mainly lignin and manganese peroxidases, are the privileged oxidoreductases for bioremediation processes. Nonetheless, an increasing diversity of laccases and peroxidase-type enzymes has been proposed for environmental technologies.
This article aims to provide an overview of these enzymes and compare their applicability in the degradation of organic pollutants.
Fundamental properties of the proteins are covered and applications towards polycyclic aromatic hydrocarbons (PAHs) and pesticides are specially focused.
Laccases are multicopper oxidases initially studied for applications in the pulp and paper industry but able to oxidize a variety of environmentally concerning compounds. Relying on O, laccases do not require peroxides nor auxiliary agents, like Mn, although suitable redox mediators are needed to attack the more recalcitrant pollutants (e.g., PAHs). True and pseudo-peroxidases use a stronger oxidant (HO) and the redox chemistry at the heme site generates high potential species that allow the oxidation of dyes and some pesticides.
Lately, research efforts have been directed to enzyme discovery, testing with micropollutants, and improving biocatalysts' stability by immobilization and protein engineering. Further understanding of the effects of natural media components and solvents on the enzymes might lead to competitive enzymatic treatments of highly toxic media.
漆酶和过氧化物酶因其在工业和环境应用中的巨大潜力而受到广泛关注。这些酶具有广泛的底物范围和强大的氧化能力。此外，使用介体或共氧化剂可以提高它们的催化活性，并将其底物范围扩展到更具抗性的化学结构。
真菌漆酶和木质素过氧化物酶，主要是木质素过氧化物酶和锰过氧化物酶，是生物修复过程中最优先的氧化还原酶。然而，越来越多的漆酶和过氧化物酶类酶已被提议用于环境技术。
本文旨在概述这些酶，并比较它们在降解有机污染物方面的应用。
涵盖了蛋白质的基本特性，并特别关注了多环芳烃（PAHs）和农药的应用。
漆酶最初是作为制浆造纸工业的应用而被研究的多铜氧化酶，但能够氧化多种对环境有影响的化合物。依赖 O 的漆酶不需要过氧化物或辅助剂（如 Mn），尽管需要合适的氧化还原介体来攻击更难降解的污染物（如 PAHs）。真正和假过氧化物酶使用更强的氧化剂（HO），并且血红素部位的氧化还原化学产生高电位物种，允许氧化染料和一些农药。
最近，研究工作的重点是酶的发现、对微污染物的测试以及通过固定化和蛋白质工程提高生物催化剂的稳定性。进一步了解天然介质成分和溶剂对酶的影响可能会导致对高毒性介质的竞争性酶处理。
