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Please use this identifier to cite or link to this item: http://dspace.bits-pilani.ac.in:8080/jspui/handle/123456789/15428
Title: Unveiling the potential of Lichtheimia ramosa AJP11 for myco-transformation of polystyrene sulfonate and its driving molecular mechanism
Authors: Panwar, Jitendra
Keywords: Biology
Synthetic plastics
Polystyrene sulfonate
Myco-transformation
Fungal proteins
Hydrophobic surface binding protein
Molecular docking
Issue Date: Jan-2023
Publisher: Elsevier
Abstract: Plastic pollution is a major environmental concern due to its deleterious effects on various ecosystems. The limitations and shortcomings of waste management strategies has led to the over-accumulation of plastic waste, mainly comprised of single-use plastics, such as polystyrene (PS). Considering the advantages of biotransformation over the other plastic disposal methods, it has become a major focus of the modern research. Biotransformation of plastics involves its microbial hydrolysis into short chain oligomers and monomers that are eventually assimilated as carbon source by the microbes leading to the release of CO2. As fungi are known to possess multifarious and highly regulated enzyme system capable of utilizing diverse nutrient sources, the present study explored the potential of Lichtheimia ramosa AJP11 towards myco-transformation of polystyrene sulfonate (PSS), a structural analogue of polystyrene (PS). During the 30-day incubation period of L. ramosa AJP11 in minimal salt medium (MSM)+1% PSS, the fungus showed 41.6% increment in its fresh weight biomass, indicating the utilization of PSS as sole carbon source. Further analysis revealed the generation of various reaction intermediates such as alkanes and fatty acids, crucial for the continuum of fungal metabolic pathways. Moreover, detection of PS oligomers such as cyclohexane and 2,4-DTBP confirmed the myco-transformation of PSS. The extracellular fungal protein profile showed considerable overexpression of a 14.4 kDa protein, characterized to be a hydrophobic surface binding (Hsb) protein, which is hypothesized to adsorb onto the PSS to facilitate its transformation. Further, in silico analysis of Hsb protein indicated it to be an amphiphilic α-helical protein with ability to bind styrene sulfonate unit via both hydrogen and hydrophobic interactions, with a binding energy of −5.02 kcal mol−1. These findings open new avenues for over expression of Hsb under controlled reactor conditions to accelerate the PS waste disposal.
URI: https://www.sciencedirect.com/science/article/pii/S0301479722021521?via%3Dihub#abs0010
http://dspace.bits-pilani.ac.in:8080/jspui/xmlui/handle/123456789/15428
Appears in Collections:Department of Biological Sciences

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