MOLECULAR INTERACTION STUDIES ON MELANOIDIN PIGMENTS WITH PEROXIDASES REVEAL PREFERENTIAL BINDING AND THEIR PLAUSIBLE ROLES IN BIOREMEDIATIONS.N. PRUTHVI AND H.G. NAGENDRAAbstract The presence of melanoidin polymers in the distillery effluent are considered as the main reason for its pitch dark brown colour and its recalcitrant property render the spent wash formidable to any easy remediation procedures. Due to the complex structure and xenobiotic nature, melanoidin rich distillery effluents when disposed into water bodies, causes severe stress on BOD, leading to rapid dip in the photosynthetic activity and dissolved oxygen contents, thus gravely affecting the aquatic life. Consumption of the food products from such aquatic sources and livestock reared in that region, in turn affect the health of humans, as the accumulation of melanoidin polymers and associated toxic ligands in the food chain would trigger skin allergies, lung ailments, and colon cancer. Therefore, rapid cost-effective treatment strategies of these distillery effluents are the need of the hour. Peroxidases present in the fungal sources, which have acclaimed bioremediation and biopulping properties, are known to bind to melanoidin polymers thereby assisting in their easy filtration. However, the molecular level of interaction of fungal enzymes with melanoidins is still unclear. Hence, docking studies with two fungal peroxidases were carried out to appreciate their efficacies of binding. The results reveal interesting patterns of association, exhibiting that the melanoidin ligands specifically bind to the coordinating residues in the targets. This knowledge would enable one to develop novel and innovative setups, towards effective in situ remediation methods.
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