Hydrophobicity Character of A-lactalbumin Nanoparticles: An Ultrasonic Study

Effect of pH and cosolvent on the stabilization of protein structure is a well established study in protein or food science. Among the various applications of proteins, the use of protein nanoparticle as drug or bioactive compound carriers is the one which is of most interest to many diverse researchers. The synthesis of such protein nanoparticles and their characterization is of prior requirement for the realization of these drug or bioactive carriers. On this basis, the present work deals with the ultrasonic analysis of hydrophobic interactions exhibited by the a-lactalbumin nanoparticle synthesized by heat treatment using acetone as desolvating agent. In order to enrich the variations in hydrophobicity, heat or temperature and cosolvent (glucose) are included in the study. The results are interpreted in terms of the interactions existing among the components and the evolved discussions reveal the bulk nature of the medium is controlled by the existing hydrophobicity interactions. The obtained results indicate that the dependency of protein denaturation on heat and the strengthening of non- covalent interactions by the cosolvent and/or the steric exclusion effect can be attributed to the structural modifications of protein.