EsteraseG (EstG) from Sphingobium sp. SM42 efficiently degraded the toxic chemical, dibutyl phthalate (DBP). In this study EstG was successfully displayed on the surface of Escherichia coli using the Pseudomonas aeruginosa outer membrane protein, OprF, as a carrier protein. EstG was fused to the C-terminus of OprF at Lys(164) resulting in export to the surface of E. coli that was detected by western blot analysis and flow cytometry, as well as immunofluorescence microscopy. The surface displayed EstG exhibited increased thermal stability, retaining 55, 43, and 39% of its original activity after 24h incubation at 45, 55, and 65 degrees C, respectively. In addition, EstG was engineered to be efficiently secreted into the culture media of Bacillus subtilis, which exhibited 8-fold higher esterase activity than cell lysates. A bacterial consortium consisting of recombinant bacteria has high potential for DBP degradation by removing almost 70% of 1 mM DBP within 5 days. (C) 2016 Elsevier Ltd. All rights reserved.