Structural and functional impacts of glycosylation-induced modifications in rabbit myofibrillar proteins

Abstract

Rabbit meat, recognized for its nutritional value, is gaining global attention. However, the inferior functional properties of rabbit myofibrillar proteins lead to quality degradation during the production process. Glycosylation represents an effective method for enhancing protein functionality. This study investigated the glycosylation modification of rabbit myofibrillar proteins. The results demonstrated that solubility of glucose-glycosylated products increased by 34 %, while the reduction capacity improved from 0.15 mg/mL to 1.6 mg/mL. The·OH free radical scavenging ability increased from 63.94 % to 94.21 %. β-Glucan-glycosylated products exhibited the highest thermal stability, and their DPPH free radical scavenging rate increased from 19.68 % to 76.21 %. Glycosylation also induced changes in protein conformation, characterized by a 10–30 °C increase in thermal denaturation peak temperature, gradual attenuation of endogenous fluorescence intensity, gradual enhancement of λmax redshift, and a 30–40 % decrease in surface hydrophobicity. Molecular docking simulations revealed that the primary interactions between glucose, lactose, and β-Glucan with myofibrillar proteins involve hydrogen bonds and van der Waals forces. In conclusion, glycosylation can effectively improve the functional properties of proteins, contributing to the development and production of high-quality, stable, and nutritious rabbit meat products.