New insights into ultrasound-assisted noncovalent nanocomplexes of β-lactoglobulin and neochlorogenic acid/cryptochlorogenic acid and its potential application for curcumin loading.

The cross-linking sites and structure of protein-polyphenol complexes are susceptible to the type, structure, weight of polyphenols under nonthermal process. The low bioavailability and poor gastrointestinal instability of curcumin (CUR) hampers its application. Hence, changes in binding mechanism, structural and functional properties between β-lactoglobulin (β-LG) with two different configurations of chlorogenic acids (neochlorogenic acids (3-CQA) and cryptochlorogenic acids (4-CQA) by non-covalent binding under ultrasonic treatment, and the potential capacity for loading CUR were researched. The binding affinity scores of β-LG-4CQA was -7.1 kcal/mol. It is higher than β-LG-3CQA (-6.8 kcal/mol), which implied that the interaction between β-LG and 4-CQA was stronger. Circular dichroism calculations showed that the sonicated complex of the β-LG and 4-CQA with a decreased content of α-helices by 5.4 %, β-sheets by 4.6 %, and an increased content of irregular curls by 8.4 % (p < 0.05). The result demonstrated ultrasound and the binding of β-LG to 3/4-CQA improved the hydrophilicity, thermal stability, and antioxidant property of β-LG. Furthermore, the embedding rate of CUR in the ultrasound-assisted β-LG-4-CQA complex could reach 71.56 %. Consistent with the structural characterization results, the CUR release rate of ULG-4-CQA + CUR complex reached 17.36 % in simulated intestinal digestion, which was 8.09 % higher than free CUR. Indicating that after embedding with protein-polyphenol complexes, the stability and bioaccessibility of CUR was improved. This study reveals the potential application of ultrasound-assisted protein-polyphenol complexes for loading CUR.