CHARACTERIZATION OF PLASTIC DEGRADATION ASSOCIATED BACTERIAL ENZYME CUTINASE THROUGH IN-SILICO TOOLS

Abstract

Plastic pollution is a crucial problem globally. It exerts negative impact on aquatic as well as human life. Bioremediation based on bacterial enzymes is an emerging and sustainable mode of plastic degradation. In current study, two plastic degrading enzymes G8GER6 and E9LVH8 from bacteria bacteria Thermobifida fusca and Thermobifida cellulosilytica were targeted for analysis. UNIPROT database was accessed to retrieve the sequences of enzymes. Followed this, enzymes were analyzed via PROPARAM and SOPMA tool and ALPHAFOLD web server. Analysis revealed the number of amino acids (319 and 262), theoretical pI (9.65 and 6.30), extinction coefficients (38390 and 36900), instability index (41.75 and 36.39), aliphatic index (79.06 and 80.50) and GRAVY values (-0.247 and -0.221) for these two enzymes. Alpha helix, extended strand and random coil content was found in the range of 64-88, 36-44 and 154-195, respectively. Both proteins exhibited tertiary structure with complex folding. Current study findings will be helpful in simulating mutations via site directed mutations that might increase binding affinity of enzyme with plastic and its degradation efficiency.