In the present study, the compost thermophile isolated from plastic rich environment was used as a source for purification and characterization of PLA depolymerase. The depolymerase activity of Bacillus licheniformis was measured at 5day interval and esterase activity of PLA depolymerase was confirmed by enzyme assay using pnitrophenyl acetate (PNPA) as substrate.The esterase activity of PLA depolymerase markedly increased from day 5, reached maximum on day 20 and showed decreased trend in the esterase activity at later stages of degradation. PLA depolymerase was purified from the culture supernatant of B.licheniformis by using ammonium sulphate fractionation and ion exchange chromatography techniques. The PLA depolymerase was purified to homogeneity with a molecular mass of 44 KDa. The PLA depolymerase has optimal activity at temperature around 50°C-60°C and at pH 6 to 7.Ethyl acetate markedly inhibited enzyme activity, whereas all other solvents like hexane, isopropanol, DMSO, ethanol, methanol, acetonitrile and acetone showed only a minor inhibition in PLA depolymerase activity.