Proteomic response of Pseudomonas aeruginosa IIPIS-8 during rapid and efficient degradation of naphthalene

• Published in: Environmental research Vol. 216; no. Pt 2; p. 114511
• Main Authors: Imam, Arfin, Suman, Sunil Kumar, Singh, Praveen, Vempatapu, Bhanu Prasad, Tripathi, Deependra, Ray, Anjan, Kanaujia, Pankaj K.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Inc 01.01.2023
• Subjects: Biodegradation; Biodegradation, Environmental; Ecosystem; First-order kinetics; Naphthalene; Naphthalenes - toxicity; Polycyclic Aromatic Hydrocarbons - metabolism; Proteome; Proteomics; Pseudomonas aeruginosa; Biodegradation; Pseudomonas aeruginosa; Naphthalene; First-order kinetics; Proteomics
• ISSN: 0013-9351; 1096-0953
• DOI: 10.1016/j.envres.2022.114511

Polycyclic aromatic hydrocarbons (PAHs) are widely distributed in the ecosystem and are of significant concern due to their toxicity and mutagenicity. Bioremediation of PAHs is a popular and benign approach that ameliorates the environment. This study investigated the biodegradation and proteome response of Pseudomonas aeruginosa IIPIS-8 for two-ringed PAH: naphthalene (NAP) to understand proteome alteration during its bioremediation. Rapid biodegradation was observed up to 98 ± 1.26% and 84 ± 1.03%, respectively, for initial concentrations of 100 mg L−1 and 500 mg L−1 of NAP. Degradation followed first-order kinetics with rate constants of 0.12 h−1 and 0.06 h−1 and half-life (t1/2) of 5.7 h and 11.3 h, respectively. Additionally, the occurrence of key ring cleavage and linear chain intermediates, 2,3,4,5,6, -pentamethyl acetophenone, 1-octanol 2-butyl, and hexadecanoic acid supported complete NAP degradation. Proteomics study of IIPIS-8 throws light on the impact of protein expression, in which 415 proteins were quantified in sequential windowed acquisition of all theoretical fragment ion mass spectra (SWATH-MS) analysis, of which 97 were found to be significantly up-regulated and 75 were significantly down-regulated by ≥ 2-fold change (p values ≤ 0.05), during the NAP degradation. The study also listed the up-regulation of several enzymes, including oxido-reductases, hydrolases, and catalases, potentially involved in NAP degradation. Overall, differential protein expression, through proteomics study, demonstrated IIPIS-8's capability to efficiently assimilate NAP in their metabolic pathways even in a high concentration of NAP.