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Bioremediation of triphenyl phosphate in river water microcosms: Proteome alteration of Brevibacillus brevis and cytotoxicity assessments
- Wei, Kun, Yin, Hua, Peng, Hui, Lu, Guining, Dang, Zhi
- The Science of the total environment 2019 v.649 pp. 563-570
- Brevibacillus brevis, amino acids, bacteria, bioaugmentation, biodegradation, biosynthesis, biphenyl, cell walls, cytotoxicity, electronic wastes, energy metabolism, flame retardants, human cell lines, humans, lipid metabolism, organophosphorus compounds, phosphates, protein synthesis, proteins, proteome, recycling, river water, toxicity testing, China
- Triphenyl phosphate (TPHP), an organophosphate flame retardant, was detected in river water samples collected from an electronic waste recycling area in Guiyu, Southern China. The concentrations of TPHP ranged from not detected to 347.2 ng/L, with an average of 138.8 ng/L. The bioaugmentation potential of Brevibacillus brevis on TPHP biodegradation by aerobic microcosms contained in river water from Guiyu was assessed. The results showed that TPHP degradation efficiency was significantly improved to 97.9% by bioaugmentation with B. brevis after 96 h incubation. A total of 182 significantly changed proteins in B. brevis were identified and quantified by isobaric tags for relative and absolute quantification (iTRAQ) in response to TPHP stress. The differentially expressed proteins were mainly associated with energy metabolism, lipid metabolism, cell wall biosynthesis, amino acid transport, and metabolism. The identification that proteins of B. brevis respond to TPHP existence provides novel insights into biodegradation mechanisms of bacteria under environmental stress. Additionally, cytotoxicity assays indicated that the degrading intermediates of TPHP, namely diphenyl phosphate and phenyl phosphate, were less cytotoxic to human HepG2 cells compared with TPHP. Collectively, these findings suggest that aerobic bioaugmentation with degrading microorganisms is a potential strategy for in situ treatment of TPHP-contaminated sites.