The toxic and recalcitrant dyes negatively impact our environment. The biological breakdowns of these toxic compounds using laccases have been explored to degrade these dyes effectively. Despite the low redox potential, compared to fungal laccases, the ability of Streptomyces laccases to work under alkaline pH against a wide range of substrates and unusual resistance to inhibitors opens up new opportunities for their commercial applications. The present study evaluated Streptomyces isolates for multicopper oxidase (MCO) production using 2,6-dimethoxyphenol (DMP), syringaldazine and guaiacol as substrates. The biochemical characterisation of purified laccase enzyme showed that the enzyme is active between 28 and 50 °C and has a pH range of 5–8, depending upon the substrates. The immobilization of the laccase showed that the beads retained their size under acidic conditions but did not exhibit any enzyme activity. The immobilized enzyme exhibited maximum activity under alkaline conditions. The alginate laccase immobilized on beads can be reused two to three times without any significant loss of activity. The potential of free and immobilized MCO from Streptomyces significantly reduced the absorption spectra of different dyes, indicating its role in dye-discoloration, which can be used for various industrial processes and industrial effluent treatment.