Investigating the structural and conformational behavior of HEWL in the presence of iron metallosurfactant and sodium oleate metallo-catanionic aggregates Article

Kaur, N, Kaur, G, Chaudhary, GR et al. (2020). Investigating the structural and conformational behavior of HEWL in the presence of iron metallosurfactant and sodium oleate metallo-catanionic aggregates . JOURNAL OF MOLECULAR LIQUIDS, 320 10.1016/j.molliq.2020.114397

cited authors

  • Kaur, N; Kaur, G; Chaudhary, GR; Yashika

authors

abstract

  • Surface-active enzymes and surface-active aggregates developed from metallosurfactant (MS), are under investigation for their complexation in an aqueous medium with the aim of development of mixtures that have potential applications in industries. Herein, the surface-active enzyme, hen egg white lysozyme (HEWL) and metallo-catanionic aggregates of hexadecyltrimethylammonium iron (II) trichloride, FeCTAC I and sodium oleate (SO) have been used. Before going for the investigation for the structural integrity of the protein, we have focused to deduce the morphology of metallo-aggregates at two different molar ratios of FeCTAC I:SO namely 70:30 and 30:70. These two molar ratios of FeCTAC I:SO show very interesting behavior by developing different morphologies namely, micelles in 70:30 and vesicles in 30:70 molar ratio, as reported from SAXS data. Further, the changes induced in the integrity of the protein by the metallo-catanionic aggregates have been potentially studied. The protein's integrity has been untangled by SDS-PAGE, UV/Visible, fluorescence spectroscopy and HEWL activity. The forces that are responsible for all the changes in the integrity of the protein are examined by extrinsic fluorescence study. Further, the effect of temperature on the activity of HEWL in the presence and absence of metallo-catanionic aggregates has also been elucidated.

publication date

  • December 15, 2020

published in

Digital Object Identifier (DOI)

volume

  • 320