Demystification of novel plastic-degrading enzymes identified from fungal genomes through integrated bioinformatics approaches.

Plastic pollution threatens lives, since only 9% of 8300 MMT of plastic has ever been recycled. Fungal enzymes offer a vital, eco-friendly solution to this crisis. Consequently, there is limited information regarding these enzymes from different fungal genomes. To find the functionalities of these proteins, several in-silico characterizations have been conducted, along with docking analyses to evaluate interactions with common plastics (LDPE, PVC, HDPE, PP, PS, PCL, Nylon, PET, DBP, DEP, and BPA). Utilizing BLASTp with AfLaccase, AnLipase, FoCutinase, and AtPeroxidase as queries, identify 56 Lac, Lip, Cu, and Per proteins from the proteomes of Aa, An, Ap, At, Fo, and Pc. Phylogram showed distinct protein groups. Domains suggest degrading capabilities. The extracellular location has indicated the position of fungal thermoplastics (TPs) breaking enzymes. GO IDs GO:0003824 and GO:0016787, beside cis-elements including ERE, CGACG, BOXLCORE, and CURECORE, suggest catalytic function. Anticipated ApLac1, ApLac3, ApLip1, and ApLip2 genes are highly expressed in C16 and lcAlk cultures and predicted Lac and Lip genes may perform identical functions due to their similarities. Cu (0 of 14) < Lip (2 of 13) < Per (5 of 11) < Lac (14 of 18) of predicted proteins have binding affinities ≥ -7 kcal/mol with BPA and other TPs. Cu < Lip < Per < Lac of Aa, An, Ap, At, Fo, and Pc indicated higher to lower active site area and volume compared to other proteins, suggesting Lac may have a high degrading capacity. This study uncovers potential enzymes that could be useful resources for future experimental research on plastic degradation.