Associate Professor South Dakota State University Brookings, SD, United States
Abstract: Bovine milk contains complex large size protein structures called caseins micelles with size ranging between 50 – 500nm, having a very open and loose structure with cavities (20 – 30nm) and channels (5nm diameter). The casein micelles are held together mostly by hydrophobic, hydrogen and electrostatic interactions and calcium phosphate bridges. A number of bioactive molecules have been hypothesized to be incorporated in the cavities and channels within the casein micelles by various processes and stabilized by hydrophobic interactions with the amphiphilic protein molecules. However, there are limited studies elucidating the interactions of casein micelles with the bioactive molecules and the binding mechanisms involved. Our research focuses on understanding the interaction of the casein micelles mostly by noncovalent interactions with a number of bioactive molecules including vitamins, drugs, and polyphenols on processing using simple mixing, ethanol and high-pressure processing. In addition, we have evaluated the factors affecting the interactions of polyphenols with milk proteins and the impact on their bioavailability and health effects. Hence, many future possibilities exist for utilizing the delivery properties of the casein micelles for incorporation in food products, as drug carriers for targeted and controlled release of bioactive compounds to benefit sensitive populations like immune-compromised, children and geriatrics.