LAUSR

Ovalbumin particles are reduced to nano size using heat treatment techniques. Their structural patterns in their native state and in their pH denatured state were attempted. Denaturation is also a part of conformation and hence conformations due to pH and glucose were analyzed using FTIR spectroscopy. The interactions behind these conformations are unraveled and the role of glucose as cosolvent in restricting the denaturation is also revealed from the observed secondary structures of ovalbumin. Further, the characterization of these synthesized nano particles reveals the extent of their applications. The obtained results indicate that consideration of ovalbumin nanoparticles seems to favor a very clear trend of protein denaturation and the observed structural modifications are the result of development of non-covalent interactions by the cosolvent molecules.