Environmental Decontamination of a Chemical Warfare Simulant Utilizing a Membrane Vesicle-Encapsulated Phosphotriesterase
Source abstract
Abstract
While technologies for the remediation of chemical contaminants continue to emerge, growing interest in green technologies has led researchers to explore natural catalytic mechanisms derived from microbial species. One such method, enzymatic degradation, offers an alternative to harsh chemical catalysts and resins. Recombinant enzymes, however, are often too labile or show limited activity when challenged with nonideal environmental conditions that may vary in salinity, pH, or other physical properties. Here, we demonstrate how phosphotriesterase encapsulated in a bacterial outer membrane vesicle can be used to degrade the organophosphate chemical warfare agent (CWA) simulant paraoxon in environmental water samples. We also carried out remediation assays on solid surfaces, including glass, painted metal, and fabric, that were selected as representative materials, which could potentially be contaminated with a CWA.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Pesticide and Herbicide Environmental Studies · Insect Resistance and Genetics · Force Microscopy Techniques and Applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Emergency Medicine, Indiana University School of Medicine, Indianapolis, Indiana 46202, United States
Center for Bio/Molecular Science & Engineering, Naval Research Laboratory, Code 6900 Washington, District of Columbia 20375, United States
National Research Council Postdoctoral Fellow, Washington, District of Columbia 20001, United States
Funding
Office of Naval Research · Defense Threat Reduction Agency
References (26)
Show source-provided references
1. 10.4061/2011/80518710.4061/2011/805187 ↗
2. 10.1007/s13205-016-0485-810.1007/s13205-016-0485-8 ↗
3. Dec, J.; Bollag, J.M., Use of Enzymes in Bioremediation. In Pesticide Biotransformation in Plants and Microorganisms, ACS Symposium Series; 2000; pp 182–193.10.1021/bk-2001-0777.ch010 ↗
4. 10.4061/2011/47519310.4061/2011/475193 ↗
5. 10.1016/j.jclepro.2012.11.00510.1016/j.jclepro.2012.11.005 ↗
6. Pushpanathan M. · 2014 · 40710.1016/B978-0-12-800021-2.00017-0 ↗
7. 10.1080/0738855060084279410.1080/07388550600842794 ↗
8. 10.1016/j.gene.2011.03.00110.1016/j.gene.2011.03.001 ↗
9. 10.1186/1475-2859-7-510.1186/1475-2859-7-5 ↗
10. Nath A. · 2014 · 45510.1016/B978-0-12-800021-2.00020-0 ↗
11. 10.1021/acsami.5b0881110.1021/acsami.5b08811 ↗
12. 10.1038/srep2486610.1038/srep24866 ↗
13. 10.1021/acsnano.5b0345910.1021/acsnano.5b03459 ↗
14. 10.1016/j.jmb.2013.10.02110.1016/j.jmb.2013.10.021 ↗
15. 10.1073/pnas.111548510910.1073/pnas.1115485109 ↗
16. 10.1039/C5CC00418G10.1039/C5CC00418G ↗
17. 10.1128/AEM.02874-0810.1128/AEM.02874-08 ↗
18. 10.1128/AEM.02947-1410.1128/AEM.02947-14 ↗
19. 10.4236/abb.2011.2302110.4236/abb.2011.23021 ↗
20. Lalain T. · 201210.21236/ADA566601 ↗
21. 10.1021/jf000486310.1021/jf0004863 ↗
22. 10.1080/0360123980937315010.1080/03601239809373150 ↗
23. 10.1007/s00253005065710.1007/s002530050657 ↗
24. 10.1016/j.cej.2016.09.04510.1016/j.cej.2016.09.045 ↗
25. 10.1371/journal.pone.009710310.1371/journal.pone.0097103 ↗
26. 10.1021/acsami.7b1976310.1021/acsami.7b19763 ↗