Bacterial surface display of metal binding peptides as whole-cell biocatalysts for 4-nitroaniline reduction

RSC Advances ◽  
2015 ◽  
Vol 5 (107) ◽  
pp. 87998-88001 ◽  
Author(s):  
Dong-Yu Tsai ◽  
Yi-Jung Tsai ◽  
Chia-Ho Yen ◽  
Chun-Yu Ouyang ◽  
Yi-Chun Yeh

Using recombinant microorganisms expressing metal binding peptides as whole-cell biocatalysts for 4-nitroaniline reduction.

1999 ◽  
Vol 65 (3) ◽  
pp. 1092-1098 ◽  
Author(s):  
Pavel Kotrba ◽  
Lucie Dolečková ◽  
Víctor de Lorenzo ◽  
Tomas Ruml

ABSTRACT Metal binding peptides of sequences Gly-His-His-Pro-His-Gly (named HP) and Gly-Cys-Gly-Cys-Pro-Cys-Gly-Cys-Gly (named CP) were genetically engineered into LamB protein and expressed in Escherichia coli. The Cd2+-to-HP and Cd2+-to-CP stoichiometries of peptides were 1:1 and 3:1, respectively. Hybrid LamB proteins were found to be properly folded in the outer membrane ofE. coli. Isolated cell envelopes of E. colibearing newly added metal binding peptides showed an up to 1.8-fold increase in Cd2+ binding capacity. The bioaccumulation of Cd2+, Cu2+, and Zn2+ by E. coli was evaluated. Surface display of CP multiplied the ability of E. coli to bind Cd2+ from growth medium fourfold. Display of HP peptide did not contribute to an increase in the accumulation of Cu2+ and Zn2+. However, Cu2+ ceased contribution of HP for Cd2+accumulation, probably due to the strong binding of Cu2+ to HP. Thus, considering the cooperation of cell structures with inserted peptides, the relative affinities of metal binding peptide and, for example, the cell wall to metal ion should be taken into account in the rational design of peptide sequences possessing specificity for a particular metal.


2000 ◽  
Vol 66 (3) ◽  
pp. 1243-1248 ◽  
Author(s):  
Patrik Samuelson ◽  
Henrik Wernérus ◽  
Malin Svedberg ◽  
Stefan Ståhl

ABSTRACT Recombinant Staphylococcus xylosus andStaphylococcus carnosus strains were generated with surface-exposed chimeric proteins containing polyhistidyl peptides designed for binding to divalent metal ions. Surface accessibility of the chimeric surface proteins was demonstrated and the chimeric surface proteins were found to be functional in terms of metal binding, since the recombinant staphylococcal cells were shown to have gained Ni2+- and Cd2+-binding capacity, suggesting that such bacteria could find use in bioremediation of heavy metals. This is, to our knowledge, the first time that recombinant, surface-exposed metal-binding peptides have been expressed on gram-positive bacteria. Potential environmental or biosensor applications for such recombinant staphylococci as biosorbents are discussed.


1998 ◽  
Vol 11 (9) ◽  
pp. 825-832 ◽  
Author(s):  
P. S. Daugherty ◽  
G. Chen ◽  
M. J. Olsen ◽  
B. L. Iverson ◽  
G. Georgiou

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e80474 ◽  
Author(s):  
Sónia Troeira Henriques ◽  
Louise Thorstholm ◽  
Yen-Hua Huang ◽  
Jennifer A. Getz ◽  
Patrick S. Daugherty ◽  
...  

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Jesica Urbina ◽  
Advait Patil ◽  
Kosuke Fujishima ◽  
Ivan G. Paulino-Lima ◽  
Chad Saltikov ◽  
...  

Abstract Electronics waste production has been fueled by economic growth and the demand for faster, more efficient consumer electronics. The glass and metals in end-of-life electronics components can be reused or recycled; however, conventional extraction methods rely on energy-intensive processes that are inefficient when applied to recycling e-waste that contains mixed materials and small amounts of metals. To make e-waste recycling economically viable and competitive with obtaining raw materials, recovery methods that lower the cost of metal reclamation and minimize environmental impact need to be developed. Microbial surface adsorption can aid in metal recovery with lower costs and energy requirements than traditional metal-extraction approaches. We introduce a novel method for metal recovery by utilizing metal-binding peptides to functionalize fungal mycelia and enhance metal recovery from aqueous solutions such as those found in bioremediation or biomining processes. Using copper-binding as a proof-of-concept, we compared binding parameters between natural motifs and those derived in silico, and found comparable binding affinity and specificity for Cu. We then combined metal-binding peptides with chitin-binding domains to functionalize a mycelium-based filter to enhance metal recovery from a Cu-rich solution. This finding suggests that engineered peptides could be used to functionalize biological surfaces to recover metals of economic interest and allow for metal recovery from metal-rich effluent with a low environmental footprint, at ambient temperatures, and under circumneutral pH.


2019 ◽  
Vol 41 (6-7) ◽  
pp. 763-777 ◽  
Author(s):  
Chang-ye Hui ◽  
Yan Guo ◽  
Lisa Liu ◽  
Hao-qu Zheng ◽  
Hong-min Wu ◽  
...  

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