Activity and thermal stability of Mycobacterium tuberculosis PE1 and PE2 proteins esterase domain in the presence of aprotic ionic liquids.
Autor: | Divya MB; School of Chemistry, University of Hyderabad, Hyderabad, Telangana 500046, India., Guruprasad L; School of Chemistry, University of Hyderabad, Hyderabad, Telangana 500046, India. Electronic address: lalitha.guruprasad@uohyd.ac.in. |
---|---|
Jazyk: | angličtina |
Zdroj: | Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy [Spectrochim Acta A Mol Biomol Spectrosc] 2020 Jan 15; Vol. 225, pp. 117477. Date of Electronic Publication: 2019 Aug 19. |
DOI: | 10.1016/j.saa.2019.117477 |
Abstrakt: | An ionic liquid (IL) is a salt in which the ions are poorly coordinated, resulting in these solvents being liquid below 100 °C or even at room temperature. ILs generally consist of large sized anions and cations, have certain unique advantageous properties and hence are considered as 'green solvents'. Thermal stability of the α/β-serine hydrolase (SH) domain in PE1 and PE2 proteins of Mycobacterium tuberculosis (M.tb) possessing esterase activity was studied in the presence of aprotic ILs consisting of imidazolium cations and anions. Addition of ILs to an aqueous solution of proteins prevented their unfolding and aggregation at higher temperatures. The thermal denaturation curve of proteins with ILs shifted to higher temperatures compared to the absence of ILs from CD spectra. The remaining activities of PE1/PE2 proteins with 1.4 M [EMIM][BF (Copyright © 2019 Elsevier B.V. All rights reserved.) |
Databáze: | MEDLINE |
Externí odkaz: |