Molecular mechanism of high-pressure processing regulates the aggregation of major royal jelly proteins

The aggregation behavior of major royal jelly proteins (MRJPs) significantly impacts their quality and nutrient bioavailability, yet studies on their aggregate regulation are limited. This study aimed to evaluate the effect of high-pressure processing (HPP) treatment on the aggregation behavior of food-derived proteins, like MRJPs, and to reveal the regulation mechanism at the molecular level. Results showed that HPP treatment, particularly at pressures of 100-200 MPa, effectively disrupted the filaments aggregation of MRJPs, resulting in smaller particle size and uniformity. Higher pressure (400-600 MPa) caused small particles to aggregate and form larger aggregates. Additionally, HPP treatment regulates aggregation behavior mainly by affecting the higher-order structure (tertiary and quaternary structures) of MRJPs, rather than by altering its secondary structure. Protein conformational dynamics based on high-pressure conditions reveal that HPP regulates MRJPs aggregation mainly by affecting interchain hydrogen bonding and hydrophobic interactions. In conclusion, this study provides valuable insights and theoretical support into the regulation mechanism of food-derived protein aggregation and supports the pre-treatment of MRJPs in the development of functional foods.

Automated summary

This study evaluated the effect of high-pressure processing on the aggregation behavior of major royal jelly proteins (MRJPs) and revealed the regulation mechanism at the molecular level. The results showed that high-pressure processing effectively disrupted the filament aggregation of MRJPs and regulated their aggregation behavior mainly by affecting the higher-order structure. This study provides valuable insights and theoretical support into the regulation mechanism of food-derived protein aggregation and supports the pre-treatment of MRJPs in the development of functional foods.