Isolation and Characterization of a Novel Laccase-Producing Bacteria Bhargavaea Beijingensis from Paper and Pulp Effluent-Treated Soil Using In Silico Approaches

Laccases (EC 1.10.3.2) are considered one of the most prominent multicopper enzymes that exhibit the inherent properties of oxidizing a range of phenolic substrates. Mostly, reported laccases have been isolated from the plants and fungi species, whereas bacterial laccases are yet to be explored. Bacterial laccases have numerous distinctive properties over fungal laccases, including stability at high temperatures and high pH. This study includes the isolation of bacteria through the soil sample collected from the paper and pulp industry; the highest laccase-producing bacteria was identified as Bhargavaea bejingensis, using 16S rRNA gene sequencing. The extracellular and intracellular activities after 24 h incubation were 1.41 U/mL and 4.95 U/mL, respectively. The laccase-encoding gene of the bacteria was sequenced; moreover, the in vitro translated protein was bioinformatically characterized and asserted that the laccase produced by the bacteria Bhargavaea bejingensis was structurally and sequentially homologous to the CotA protein of Bacillus subtilis. The enzyme laccase produced from B. bejingensis was classified as three-domain laccase with several copper-binding residues, where a few crucial copper-binding residues of the laccase enzyme were also predicted.