Comparative analysis among the degradation potential of enzymes obtained from Escherichia coli against the toxicity of sulfur dyes through molecular docking.

Autor: Naveed M; Department of Biotechnology, Faculty of Science and Technology, 66901 University of Central Punjab , Lahore 54000, Pakistan., Salah Ud Din M; Department of Biotechnology, Faculty of Science and Technology, 66901 University of Central Punjab , Lahore 54000, Pakistan., Aziz T; Laboratory of Animal Health Food Hygiene and Quality, 37796 University of Ioannina , Arta 47132, Greece., Javed T; Department of Biotechnology, Faculty of Science and Technology, 66901 University of Central Punjab , Lahore 54000, Pakistan., Miraj Khan S; Department of Biotechnology, Faculty of Science and Technology, 66901 University of Central Punjab , Lahore 54000, Pakistan., Naveed R; Department of Biotechnology, Faculty of Science and Technology, 66901 University of Central Punjab , Lahore 54000, Pakistan., Ali Khan A; Department of Biotechnology, 66714 University of Malakand , Chakdara 18800, Pakistan., Alharbi M; Department of Pharmacology and Toxicology, 37850 King Saud University , Riyadh 11461, Saudi Arabia.
Jazyk: angličtina
Zdroj: Zeitschrift fur Naturforschung. C, Journal of biosciences [Z Naturforsch C J Biosci] 2024 Apr 26; Vol. 79 (7-8), pp. 221-234. Date of Electronic Publication: 2024 Apr 26 (Print Publication: 2024).
DOI: 10.1515/znc-2024-0072
Abstrakt: The common bacterium Escherichia coli has demonstrated potential in the field of biodegradation. E. coli is naturally capable of biodegradation because it carries a variety of enzymes that are essential for the breakdown of different substances. The degradation process is effectively catalyzed by these enzymes. The collaborative effects of  E. coli 's aryl sulfotransferase, alkanesulfonate moonoxygenase, and azoreductase enzymes on the breakdown of sulfur dyes from industrial effluents are investigated in this work. ExPASY ProtParam was used to confirm the stability of the enzyme, showing an instability index less than 40. We determined the maximum binding affinities of these enzymes with sulfur dye pollutants - 1-naphthalenesulfonic acid, sulfogene, sulfur green 3, sulfur red 6, sulfur red 1, sulfur yellow 2, thianthrene, thiazone, and thional - using comparative molecular docking. Significantly, the highest binding affinity was shown by monooxygenase (-12.1), whereas aryl sulfotransferase and azoreductase demonstrated significant energies of -11.8 and -11.4, respectively. The interactions between proteins and ligands in the docked complexes were examined. To evaluate their combined effects, co-expression analysis of genes and enzyme bioengineering were carried out. Using aryl sulfotransferase, alkanesulfonate monooxygenase, and azoreductase, this study investigates the enzymatic degradation of sulfur dye pollutants, thereby promoting environmentally friendly and effective sulfur dye pollutant management.
(© 2024 the author(s), published by De Gruyter, Berlin/Boston.)
Databáze: MEDLINE