Proteome analysis of acrylamide-induced proteins in a novel acrylamide-degrader Enterobacter aerogenes by 2D electrophoresis and MALDI-TOF-MS

Despite tremendous advances in understanding the microbial degradation of acrylamide, reports on the nature of the two-dimensional protein patterns for acrylamide-degrading bacteria are not yet available. This work, focusing on the acrylamide-inducible proteins, studied the response of Enterobacter aerogenes, a novel acrylamide-degrading bacterium, to acrylamide. Proteome analysis was applied using 2D-polyacrylamide gel electrophoresis and matrixassisted laser desorption/ionisation-time of flight mass spectrometry to identify proteins differentially expressed from E. aerogenes grown on acrylamide. Six protein homologues with amidohydrolase, urease accessory protein, quaternary ammonium compound resistance proteins, dipeptide transport protein, Omp36 osmoporin and large conductance mechanosensitive channel proteins (MscL) are seemingly involved in acrylamide stress response and its degradation. Five proteins identified as GroEL-like chaperonin, ArsR-transcriptional regulator, Ts- and Tu-elongation factor and trigger factor and four proteins (phosphoglycerate kinase, ATP synthase β-subunit, malate dehydrogenase and succinyl-CoA synthetase α-subunit) responsive for the adaption of E. aerogenes in the presence of acrylamide.