Modification of soybean lipophilic protein based on pH-shifting and high-pressure homogenization: Focus on structure, physicochemical properties and delivery vehicle

High-pressure homogenization and pH-shifting can be used to modify soybean lipophilic protein (SLP), and to enhance its ability to deliver vitamin B12. The structural changes of SLP were analyzed by multispectral techniques and the results showed that secondary and tertiary structures of SLP were altered by modification. The modification unfolded the SLP structure, released more free hydrogen ions, and increased positive charge density on the protein surface. Also, the solubility of modified SLP increased by maximum of 34.75 %. Furthermore, molecular docking showed that complexes were formed between SLP and vitamin B12 mainly through hydrogen bonding and hydrophobic interactions, and the encapsulation rate of modified SLP was maximally increased by 2.3 %. In vitro digestion showed that modified SLP enhanced stability and bioaccessibility of vitamin B12. This study provides theoretical basis for modification of SLP and effective delivery of bioactive substances.