Development of bisphenol A-removing recombinant Escherichia coli by monomeric and dimeric surface display of bisphenol A-binding peptide

• Published in: Bioprocess and biosystems engineering Vol. 41; no. 4; pp. 479 - 487
• Main Authors: Maruthamuthu, Murali kannan, Hong, Jiyeon, Arulsamy, Kulandaisamy, Somasundaram, Sivachandiran, Hong, SoonHo, Choe, Woo-Seok, Yoo, Ik-Keun
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.04.2018; Springer Nature B.V
• Subjects: Adsorptivity; Asparagine; Binding; Biotechnology; Bisphenol A; Chemistry; Chemistry and Materials Science; E coli; Environmental Engineering/Biotechnology; Escherichia coli; Food Science; Industrial and Production Engineering; Industrial Chemistry/Chemical Engineering; Molecular docking; Peptides; Research Paper; Serine; Wastewater; Bisphenol A; Peptide surface display; Adsorption; ATM thermal paper; E. coli
• ISSN: 1615-7591; 1615-7605
• DOI: 10.1007/s00449-017-1882-z

Peptide-displaying Escherichia coli cells were investigated for use in adsorptive removal of bisphenol A (BPA) both in Luria–Bertani medium including BPA or ATM thermal paper eluted wastewater. Two recombinant strains were constructed with monomeric and dimeric repeats of the 7-mer BPA-binding peptide (KSLENSY), respectively. Greater than threefold increased adsorption of BPA [230.4 µmol BPA per g dry cell weight (DCW)] was found in dimeric peptide-displaying cells compared to monomeric strains (63.4 µmol per g DCW) in 15 ppm BPA solution. The selective removal of BPA from a mixture of BPA analogs (bisphenol F and bisphenol S) was verified in both monomeric and dimeric peptide-displaying cells. The binding chemistry of BPA with the peptide was assumed, based on molecular docking analysis, to be the interaction of BPA with serine and asparagine residues within the 7-mer peptide sequence. The peptide-displaying cells also functioned efficiently in thermal paper eluted wastewater containing 14.5 ppm BPA.