Micellar casein were constructed to improve the encapsulation efficiency of algae oil docosahexaenoic acid by transglutaminase-coupled phosphoserine peptide chelating with Ca²

Micelle systems using safe food-grade biopolymers are of particular interest for the encapsulation and delivery of nutrition components. Micellar casein (MC) was assembled using transglutaminase (TGase) to couple with phosphoserine peptide, which enhance the stability of docosahexaenoic acid (DHA) from algae oil. The mechanism behind the construction of MC-phosphoserine peptide and the encapsulation of DHA was explored. The results showed that the average particle size of the MC-phosphoserine peptide was 155.09 nm, when the mass ratio of polypeptide was 3 %, TGase activity was 4.5 U and pH 6.5. The recombinant MC-phosphoserine peptide system can improve the emulsification and digestive stability of DHA compared to the control MC. Chelation interaction between phosphoserine peptide and MC played an important role in increasing the stabilization reassembly MC. The phosphoserine peptide high calcium-binding capacity enhances encapsulation efficiency and digestion sustained-release in self-assembled micelles for fat-soluble substances.