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A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-<i>tert</i>-butylphenol and proteomic changes in the degrader<i>Pseudomonas aeruginosa</i>san ai
Summary
Researchers investigated the biodegradation of the plastic additive 2,6-di-tert-butylphenol (2,6-DTBP) by Pseudomonas aeruginosa strain san ai under varying pH, temperature, concentration, and inoculum conditions, finding efficient degradation (up to 100%) across a pH range of 5-8 at higher temperatures. Proteomic analysis revealed cellular changes associated with 2,6-DTBP exposure, identifying metabolic pathways involved in breakdown of this hazardous aquatic toxicant.
The <i>Pseudomonas aeruginosa</i> san ai strain was investigated for its capability to degrade the 2,6-di-<i>tert</i>-butylphenol (2,6-DTBP) plastic additive, a hazardous and toxic substance for aquatic life. This investigation was performed under different parameter values: 2,6-DTBP concentration, inoculum size, pH, and temperature. The GC-MS study showed that <i>P. aeruginosa</i> efficiently degraded 2,6-DTBP in the pH range of 5-8 at higher temperatures. Under exposure to 2,6-DTBP concentrations of 2, 10, and 100 mg L<sup>-1</sup>, the strain degraded by 100, 100, and 85%, respectively, for 7 days. Crude enzyme preparation from the biomass of <i>P. aeruginosa</i> san ai showed higher efficiency in 2,6-DTBP removal than that shown by whole microbial cells. Gene encoding for the enzymes involved in the degradation of aromatic compounds in <i>P. aeruginosa</i> san ai was identified. To complement the genomic data, a comparative proteomic study of <i>P. aeruginosa</i> san ai grown on 2,6-DTBP or sunflower oil was conducted by means of nanoLC-MS/MS. The presence of aromatic substances resulted in the upregulation of aromatic ring cleavage enzymes, whose activity was confirmed by enzymatic tests; therefore, it could be concluded that 2,6-DTBP might be degraded by <i>ortho</i>-ring cleavage. A comparative proteomics study of <i>P. aeruginosa</i> san ai indicated that the core molecular responses to aromatic substances can be summarized as the upregulation of proteins responsible for amino acid metabolism with emphasized glutamate metabolism and energy production with upregulated enzymes of glyoxylate bypass. <i>P. aeruginosa</i> san ai has a high capacity to efficiently degrade aromatic compounds, and therefore its whole cells or enzymes could be used in the treatment of contaminated areas.
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