DNA shuffling to improve crude-water interfacial activity in biosurfactants with OmpA protein of Escherichia coli .

Autor:	Nuñez Velez VL; Department of Chemical and Food Engineering, Universidad de los Andes, Bogotá, Cundinamarca, Colombia., Villamizar Gomez LD; Department of Chemical and Food Engineering, Universidad de los Andes, Bogotá, Cundinamarca, Colombia., Mendoza Ospina JE; Department of Chemical and Food Engineering, Universidad de los Andes, Bogotá, Cundinamarca, Colombia., Hayek-Orduz Y; Department of Chemical and Food Engineering, Universidad de los Andes, Bogotá, Cundinamarca, Colombia., Fernandez-Niño M; Department of Bioorganic Chemistry, Leibniz-Institute of Plant Biochemistry, Hale, Germany., Restrepo Restrepo S; Department of Chemical and Food Engineering, Universidad de los Andes, Bogotá, Cundinamarca, Colombia., Álvarez Solano ÓA; Department of Chemical and Food Engineering, Universidad de los Andes, Bogotá, Cundinamarca, Colombia., Reyes Barrios LH; Department of Chemical and Food Engineering, Universidad de los Andes, Bogotá, Cundinamarca, Colombia., Gonzalez Barrios AF; Department of Chemical and Food Engineering, Universidad de los Andes, Bogotá, Cundinamarca, Colombia.
Jazyk:	angličtina
Zdroj:	PeerJ [PeerJ] 2024 Dec 03; Vol. 12, pp. e17239. Date of Electronic Publication: 2024 Dec 03 (Print Publication: 2024).
DOI:	10.7717/peerj.17239
Abstrakt:	Surfactants are molecules derived primarily from petroleum that can reduce the surface tension at interfaces. Their slow degradation is a characteristic that could cause environmental issues. This and other factors contribute to the allure of biosurfactants today. Progress has been made in this area of research, which aims to satisfy the need for effective surfactants that are not harmful to the environment. In previous studies, we demonstrated the surface tension activity of the Escherichia coli transmembrane protein OmpA. Here, we carried out DNA shuffling on ompA to improve its interfacial activity. We evaluated changes in interfacial tension when exposing mutants to a water-oil interface to identify the most promising candidates. Two mutants reached an interfacial tension value lower (9.10 mN/m and 4.24 mN/m) than the original protein OmpA (14.98 mN/m). Since predicted isoelectric point values are far from neutral pH, the charge of the protein was a crucial factor in explaining the migration of proteins towards the interface. Low molecular weight mutants did not exhibit a significant difference in their migration to the interface. Competing Interests: The authors declare there are no competing interests. (©2024 Nuñez Velez et al.)
Databáze:	MEDLINE
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