Isolation and purification of esterase enzyme from marine bacteria associated with biodegradation of polyvinyl chloride (PVC)

Abstract

Polyvinyl chloride (PVC) is the third most produced synthetic plastic and releases the most harmful and lethal environmental component after incineration and landfilling. Few studies on microbial degradation of PVC have been reported but very little knowledge about the enzymes. In the present study, esterase enzyme was isolated and partially purified from marine bacterial isolates (T-1.3, BP-4.3 and S-237 identified as Vibrio sp., Alteromonas sp., and Cobetia sp., respectively) having the capability of PVC degradation. Initially, a plate assay was carried out for testing esterase production by studying bacteria using 1-naphthyl acetate as substrate. Enzyme assay showed higher production of esterase i.e. 0.57 U mL⁻¹ (2nd day), 0.46 U mL⁻¹ (2nd day) and 0.55 U mL⁻¹ (5th day) by bacterial isolate Vibrio sp., Alteromonas sp. and Cobetia sp., respectively incubated with PVC. Other enzymes like lipase, laccase and manganese peroxidase were much less or negligible compared to esterase enzyme production. Sephadex G-50 column purification had shown 58.62, 42.35 and 223.70 units mg⁻¹ of a specific activity by esterase for bacterial isolates Vibrio sp., Alteromonas sp. and Cobetia sp., respectively. Further, Sephadex G-50 column purification removed all the contamination and gave a clear appearance of the band at 38, 20 and 20 KD for bacterial isolates Vibrio sp., Alteromonas sp., and Cobetia sp., respectively. Esterase has shown maximum stability at a range of pH between 6.0 to 7.5, temperature between 30 to 35 °C and salinity concentration between 3 to 3.5 M for all bacterial isolates. In conclusion, esterase enzyme has promising potential to degrade PVC which can contribute to the decline the plastic pollution in an eco-friendly manner from the environment.