Oxidoreductases are a family of enzymes that have a role in various reduction, oxidation, and oxyfunctionalization reactions. They cleave chemical bonds to facilitate electron transfer from a reduced organic substrate (donor) to another chemical compound (acceptor). There are twenty-two subclasses of oxidoreductases including dehydrogenases, oxidases, mono- and di-oxygenases, peroxidases, laccases, reductases, and hydroxylases. The literature survey reviews recent discoveries and developments in the field of oxidoreductases, with particular emphasis on laccases, catalases, dehydrogenases, and lytic polysaccharide monooxygenases, during the past decade. The review also focuses on some of the common assay methods that are in use for their detection as well as some of their biotechnological applications. Experimental studies were carried out to understand the properties of laccase and catalase present in T. emersonii. Studies of laccase in T. emersonii indicated that there was only laccase present with an acidic pH optimum of pH 3.0 and temperature optimum of 40 ̊C. Studies of catalase in T. emersonii indicated that multiple catalase isoforms were present with pH optima of 4.0, 5.0, 7.0, and 8.0 and a temperature optimum of 50 ̊C. Furthermore, the use of copper sulphate was advantageous to increasing laccase production in fermentation culture. However, from the experiments conducted, it was also observed that copper sulphate had a negative impact on catalase activity. Mass spectrometry analyses were also carried out to investigate the impact of copper sulphate on protein expression, protein interaction, and protein modification.