Differential Protein Expression in Shewanella seohaensis Decolorizing Azo Dyes

Background: Microbial remediation is an ecologically safe alternative to controlling environmental pollution caused by toxic aromatic compounds including azo dyes. Marine bacteria show excellent potential as agents of bioremediation. However, a lack of understanding of the entailing mechanisms of microbial degradation often restricts its wide-scale and effective application. Objective: To understand the changes in a bacterial proteome profile during azo dye decolorization. Method: In this study, we tested a Gram-negative bacterium, Shewanella seohaensis NIODMS14 isolated from an estuarine environment and grown in three different azo dyes (Reactive Black 5 (RB5), Reactive Green 19 (RG19) and Reactive Red 120 (RR120)). The unlabeled bacterial protein samples extracted during the process of dye decolorization were subject to mass spectrometry. Relative protein quantification was determined by comparing the resultant MS/MS spectra for each protein. Results: Maximum dye decolorization of 98.31% for RB5, 91.49% for RG19 and 97.07% for RR120 at a concentration of 100 mg L-1 was observed. The liquid chromatography-mass spectrometry - Quadrupole Time of Flight (LCMS-QToF) analysis revealed that as many as 29 proteins were up-regulated by 7 hours of growth and 17 by 24 hours of growth. Notably, these were common across the decolorized solutions of all three azo dyes. In cultures challenged with the azo dyes, the major class of up-regulated proteins was cellular oxidoreductases and an alkyl hydroperoxide reductase (SwissProt ID: A9KY42). Conclusion: The findings of this study on the bacterial proteome profiling during the azo dye decolorization process are used to highlight the up-regulation of important proteins that are involved in energy metabolism and oxido-reduction pathways. This has important implications in understanding the mechanism of azo dye decolorization by Shewanella seohaensis.