Aggregation and Growth Mechanism of Ovalbumin and Sodium Carboxymethylcellulose Colloidal Particles under Thermal Induction.

Ovalbumin (OVA)/sodium carboxymethylcellulose (CMC) colloidal particles were prepared with different compactness and morphologies by regulating the interaction between proteins and polysaccharides during heating. Electrostatic interactions between the amine groups of OVA (-NH) and carboxyl groups of CMC (-COO) enhanced complex formation. The protein conformation change benefited the hydrophobic interaction between the particles. Proteins in colloidal particles were unfolded/folded under thermal induction to form aggregates having more β-sheet structures. When the OVA/CMC ratio was 1:2, the initially loosely connected OVA/CMC aggregation changed into a uniform sphere between 25 and 90 °C. The mass ratio of OVA to CMC within the final colloidal particle (90 °C) was about 1:1.4. The OVA/CMC particle stability was maintained with hydrogen bonding, hydrophobicity, and disulfide bond. When OVA levels were predominant, OVA and CMC developed an approximately hollow sphere. Moreover, the final colloidal particle composition showed the OVA-to-CMC ratio as 3:1 (w/w). OVA bound into colloidal particle pores to increase compactness. Moreover, OVA and CMC bound to the colloidal particle while the particle shrank, thereby increasing the compactness of colloidal particles. There was a significant decrease in ABTS scavenging activity of curcumin compared with that of the particles with a ratio of 1:2. Thus, the rational adjustment of the structure of colloidal particles could effectively enhance their functional characteristics, providing a new way for the controlled release of the active ingredients.