Encapsulation of rutin in protein nanoparticles by pH-driven method: impact of rutin solubility and mechanisms.

BACKGROUND

The use of rutin in the food industry is limited by its poor solubility. Encapsulation can be used as an effective way to improve polyphenol solubility. Proteins with high safety, biocompatibility and multiple binding sites are known as the most promising encapsulating carriers. Therefore, the improvement of rutin solubility by pH-driven encapsulation of rutin in soy protein isolate (SPI) nanoparticles, as well as the form of rutin after encapsulation and rutin-protein binding index were investigated.

RESULTS

SPI had a high encapsulation efficiency (87.5%) and loading amount (10.6%) for rutin. When the mass ratio of protein to rutin was 5:1, the highest concentration of rutin in solution was 3.27 g L , which was a 51.57-fold increase compared to the original rutin. At this situation, rutin transformed from crystalline to amorphous form. During the formation of nanoparticles, SPI was in a dynamic change of unfolding and refolding. Rutin deprotonated in alkaline conditions increasing its solubility and bound to protein to form nanoparticles during the process of returning to neutral. Hydrophobic interactions and hydrogen bonding promoted the formation of the nanoparticles and there were at least 1-2 binding sites between rutin and each SPI molecule.

CONCLUSION

The results suggested that encapsulation of rutin in protein nanoparticles can effectively increase the solubility of rutin. This study may provide important information for the effective utilization of polyphenol functional foods. © 2023 Society of Chemical Industry.