Effect of Molecular Weight on the Structural and Emulsifying Characteristics of Bovine Bone Protein Hydrolysate

The emulsifying capacity of bovine bone protein extracted using high-pressure hot water (HBBP) has been determined to be good. Nevertheless, given that HBBP is a blend of peptides with a broad range of molecular weights, the distinction in emulsifying capacity between polypeptide components with high and low molecular weights is unclear. Therefore, in this study, HBBP was separated into three molecular weight components of 10-30 kDa (HBBP 1), 5-10 kDa (HBBP 2), and <5 kDa (HBBP 3) via ultrafiltration, and the differences in their structures and emulsifying properties were investigated. The polypeptide with the highest molecular weight displayed the lowest endogenous fluorescence intensity, the least solubility in an aqueous solution, and the highest surface hydrophobicity index. Analysis using laser confocal Raman spectroscopy showed that with an increase in polypeptide molecular weight, the α-helix and β-sheet contents in the secondary structure of the polypeptide molecule increased significantly. Particle size, rheological characteristics, and laser confocal microscopy were used to characterize the emulsion made from peptides of various molecular weights. High-molecular-weight peptides were able to provide a more robust spatial repulsion and thicker interfacial coating in the emulsion, which would make the emulsion more stable. The above results showed that the high-molecular-weight polypeptide in HBBP effectively improved the emulsion stability when forming an emulsion. This study increased the rate at which bovine bone was utilized and provided a theoretical foundation for the use of bovine bone protein as an emulsifier in the food sector.