A study of the conformational changes of β-lactoglobulin in the vicinity of critical point of binary mixed solvents

Abstract

Most of the protein is entangled in the upper IB rich phase.

The attenuating ability of deep eutectic solvents towards the carboxylated multiwalled carbon nanotubes induced denatured β-lactoglobulin structure

“…4,13,69,75 As mentioned before, for Blg, there are two Trp residues (Trp-19 and Trp-61), among which Trp-19 is majorly responsible for the intrinsic fluorescence of the protein. 9,76 The changes in the fluorescence intensity (I max ) and the wavelength maxima (l max ) are essential evidence of the protein structural disturbance. The changes in the emission spectra are closely related to protein conformation alterations.…”

“…The alterations in these Trp residues are majorly responsible for the structural changes in the protein. 4,9 The 3-D conformation of Blg is quite sensitive and its in vitro stabilization depends on the biomolecular interactions with co-solvents. Therefore, it is an essential task to understand these specific interactions causing perturbations in the protein structure.…”

“…The native conformation of biomolecules remains intact in the presence of certain co-solvents. 4,9,[12][13][14][15] The addition of cosolvents is an easy and efficient method for improving the stability of proteins against harsh conditions like high temperature, pH and denaturants. In this context, deep eutectic solvents (DESs) with their unique properties and easy preparation have gained immense attention in various fields covering organic catalysis, biotransformation, and molecular extractions, which are of special interest for both pharmaceutical and biotechnological industries.…”