Abstract
This study aimed to explore the interaction mechanism between soybean lipophilic protein (LP) and vitamin B12 and the potential of LP as a vitamin B12 carrier. The results of spectroscopy indicated that the interaction between vitamin B12 and LP changed the conformation of LP and exposed hydrophobic groups largely. The results of molecular docking revealed that vitamin B12 interacted with LP through a hydrophobic pocket embedded on the surface of LP. With the enhancement of the interaction between LP and vitamin B12, the particle size of the LP-vitamin B12 complex gradually decreased to 588.31nm and the absolute value of zeta potential gradually increased to 26.82mV. Meanwhile, the LP-vitamin B12 complex showed excellent physicochemical properties and digestive characteristics. The present work enriched the means of vitamin B12 protection and provided a theoretical basis for applying the LP-vitamin B12 complex in food systems.
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