Affinity study of -lactalbumin nanoparticles in a mixed solvent environment using Laplace transform technique

ABSTRACT. Effect of pH and cosolvent on the stabilization of protein structure is a well established study in protein or food science. Of the various interesting applications of protein nanoparticles, making it as a drug or bioactive compound carrier is of vital importance. This application of protein nanoparticle demands the affinity priority of protein with the available components of the medium. The basis of such studies lies in the synthesis of such protein nanoparticles and their characterizations. Secondly the knowledge of priority in affinity of protein to a particular solvent is essential. On this basis, the present work deals with the ultrasonic analysis of hydophobic interactions exhibited by the α-lactalbumin nanoparticle synthesised by heat treatment using acetone as desolvating agent. In order to enrich the variations in hydrophobicity, pH and cosolvent (fructose) are included in the study. The results are compared with one of our earlier work and are interpreted in terms of the interactions existing among the components and the evolved discussions reveal that the bulk nature of the medium is controlled by the existing hydrophobicity interactions. Further, as a novel attempt, the preference of protein particle to interact with a particular solvent in mixed solvent environment is elucidated using Laplace transform technique. This approach is expected to torch light in protein science in fixing the most desirable solvent in mixed solvent environment.                     KEY WORDS: a-Lactalbumin, Fructose, Laplace Transform, Diffusion, Hydrophobic interactions   Bull. Chem. Soc. Ethiop. 2021, 35(3), 659-668. DOI: https://dx.doi.org/10.4314/bcse.v35i3.16