Abstract
One of the utmost man-made problems faced today has been the ever-increasing plastic waste filling the world. It accounts for an estimated 20–30% (by volume) of municipal solid waste in landfill sites worldwide. Research on plastic biodegradation has been steadily growing over the past four decades. Several fungi have been identified that produce enzymes capable of plastic degradation in various laboratory conditions. This paper presents a study that determined the ability of fungi to degrade low molecular weight polyvinyl chloride (PVC) by the enzyme laccase. We have isolated a fungal species, Cochliobolus sp., from plastic dumped soils and they were cultured on Czapek Dox Agar slants at 30°C. The effectiveness of this fungal species on the degradation of commercial low molecular weight polyvinyl chloride (PVC) was studied under laboratory conditions. Significant differences were observed from the FTIR, GC-MS, and SEM results in between control and Cochliobolus sp. treated PVC.
Highlights
Laccases (EC 1.10.3.2) are multicopper enzymes belonging to the group of blue oxidases which exist widely in nature and are defined in the Enzyme Commission (EC) nomenclature as oxidoreductases which oxidize diphenols and allied substances and use molecular oxygen as an electron acceptor [1, 2]
The majority of laccases have been isolated from higher fungi like Trametes spp., Cerrena maxima, Coriolopsis polyzona, Lentinus tigrinus and Pleurotus eryngii, and so forth, and laccases occur in saprophytic ascomycetes such as Myceliophthora thermophila and Chaetomium thermophile and are involved in the humification process of composts [6,7,8,9,10,11,12,13]
FTIR and GC-MS results from the present investigation indicate that polyvinyl chloride (PVC) was degraded at significant level in this present study. This investigation established the robust low molecular weight PVC degradation activity under lab conditions in which the synthetic polymer served as the only carbon source for the fungus, Cochliobolus sp
Summary
Laccases (EC 1.10.3.2) are multicopper enzymes belonging to the group of blue oxidases which exist widely in nature and are defined in the Enzyme Commission (EC) nomenclature as oxidoreductases which oxidize diphenols and allied substances and use molecular oxygen as an electron acceptor [1, 2]. The ability of laccases to oxidize a broad range of phenolic compounds employed in numerous industrial sectors has amplified their biotechnological potential. The white-rot fungal organisms are used in biodegradation processes and the oxidative ability of these fungi is related to their extracellular and intracellular enzymatic system. Their nonspecific enzymatic system allows them to degrade a wide range of pollutants resistant to other microorganisms [14]. Two major steps have been developed for use of white-rot fungi for degradation of pollutants such as dyes, plastics, pesticides, chlorophenolic compounds, and nonphenolic compounds [15]. The main advantage of fungi in the process of degradation lies in the broad range of enzymes produced and the further transformation of the intermediate
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