Screening and characterization of Lignolytic Enzymes Produced by Escherichia coli exposed to polyethylene

Several research studies has opined lignolytic enzymes to perform significant roles in bioremediation of polyethylene. However studies unveiling the physicochemical properties of these pivotal group of enzymes are limited. Hence, this study focused on screening and characterizing managanese peroxidase and laccase produced by Escherichia coliisolated from plastic polluted site under exposure to polyethylene based mineral medium. The result showed that Escherichia coli produced optimum managanese peroxidase and laccase activities on the third day. Study of their physicochemical properties revealed that managanese peroxidase activity was optimum and stable at pH 3.0 and pH 5.0 while laccase activity was optimum and stable at pH 9.0 and pH 7.0. managanese peroxidase displayed optimum temperature and stability at 40°C. While laccase displayed optimum temperature at 60°C and was most stable at 50°C. Escherichia coli produced thermostable lignolytic enzymes that were either optimum at acidic or alkaline region making it activity relevant for biodegradation of polyethylene either in acidic or alkaline medium, therefore it can be utilized for polyethylene biodegradation.