BACKGROUND: Laccases are multicopper oxidases that are able to oxidize various aromatic or nonaromatic compounds owing to their multifarious applications. However, till now only a few bacterial laccases have been isolated and characterized. Hence there is an urgent need to study an extracellular thermo-alkali stable laccase. RESULTS: In the present study, an extracellular thermo-alkali stable laccase was produced from Pseudomonas sp. S2 in a 100 L bioreactor using agro waste (potato peel). Production was 17-fold higher than in the control. The enzyme (S2LAC) was purified 12.16 +/- 1.6-fold to homogeneitywith specific activity of 1089.70 +/- 16.8 U mg(-1) and molecular mass of 38 kDa. The temperature and pH for maximum enzyme activity were 80 degrees C and 9.0, respectively. The metal ions Na+, K+, Pb+2, Ca+2, Cu+2 and Co+2 enhanced enzyme activity. The purified enzyme showed maximum specificity to Pyrogallol > PPD > L-DOPA > Hydroquinone. The S2LAC was able to degrade organ-phosphorous pesticide including dichlorophos, chlorpyrifos, monocrotophos and profenovos up to 45.99 +/- 0.3%, 80.56 +/- 0.6%, 75.45 +/- 1.3%, 81.84 +/- 0.6%, respectively, in the absence of any mediator. CONCLUSION: S2LAC produced using agro waste was stable and capable of degrading organophosphorous pesticides making it attractive for industrial applications. (C) 2017 Society of Chemical Industry.