The heterologous expression of the gene LACP83 (encoding a laccase) from Pleurotus ostreatus in Escherichia coli was characterized. The laccase enzyme activity and kinetics of bacterial growth with an inducer (IPTG) and without inducer were determined. The maximum enzymatic activity was observed at 7 h post induction with a value of 3740 ± 342 U/L, which was similar to that reported for the native strain of P. ostreatus at 144 h of culture. Furthermore, the induction of laccase with IPTG reduced the specific growth rate of recombinant E. coli BL21 by approximately 50%. These results support the use this system for the recombinant production of the enzyme on an industrial scale.