Studies on the interactional characterization of major royal jelly proteins with cyanidin-3-O-glucoside and their effect on blueberry anthocyanin extracts stability
Fangfang Ning, Mingxin Ma, Jie Huang, Xinhao Jiang, Wu Sun, Guoqiang Zhang
Abstract
The effects of major royal jelly proteins (MRJPs) on the stability of blueberry anthocyanins under various processing conditions were investigated. The results indicate that MRJPs exert a protective effect on the stability of blueberry anthocyanins when exposed to light, sucrose, vitamin C (VC), and heat. Building on these findings, fluorescence spectroscopy, Fourier transform infrared spectroscopy (FITIR), circular dichroism (CD) and other techniques were employed to explore the interaction mechanisms between MRJPs and Cyanidin-3-O-glucoside (C3G). The fluorescence results reveal that the interactions between MRJPs and C3G occur via a static quenching process. FTIR and CD spectral analyses further indicated C3G binding induces conformational changes in MRJPs’ secondary structure, characterized by reduced α-helix content and increased β-sheet composition. Furthermore, molecular simulation docking indicates that MRJPs can bind to C3G and encapsulate C3G molecules, thereby providing a basis for MRJPs to enhance the stability of blueberry anthocyanins. These findings establish the role of MRJPs in preserving anthocyanins and in the development of functional natural colorants for the food industry. • MRJPs exert a protective effect on the stability of blueberry anthocyanins. • MRJPs are thermostable proteins, particularly MRJP1 with intrinsic disorder, may stabilize anthocyanins in thermal stress. • MRJPs are glycoproteins, with all MRJPs possessing 1–8 predicted N-glycosylation sites.