Investigation of soybean lipophilic proteins as carriers for vitamin B12: Focus on interaction mechanism, physicochemical functionality, and digestion characteristics.

[Display omitted] • Vitamin B 12 promoted the structural change and hydrophobic groups exposure of LP. • Vitamin B 12 binded to the hydrophobic pocket on the surface of LP. • LP increased the UV stability of vitamin B 12. • LP-vitamin B 12 complex exhibited higher pH stability. • LP-vitamin B 12 complex exhibited excellent digestion properties. This study aimed to explore the interaction mechanism between soybean lipophilic protein (LP) and vitamin B 12 and the potential of LP as a vitamin B 12 carrier. The results of spectroscopy indicated that the interaction between vitamin B 12 and LP changed the conformation of LP and exposed hydrophobic groups largely. The results of molecular docking revealed that vitamin B 12 interacted with LP through a hydrophobic pocket embedded on the surface of LP. With the enhancement of the interaction between LP and vitamin B 12 , the particle size of the LP–vitamin B 12 complex gradually decreased to 588.31 nm and the absolute value of zeta potential gradually increased to 26.82 mV. Meanwhile, the LP–vitamin B 12 complex showed excellent physicochemical properties and digestive characteristics. The present work enriched the means of vitamin B 12 protection and provided a theoretical basis for applying the LP–vitamin B 12 complex in food systems. [ABSTRACT FROM AUTHOR]