Abstract
Abstract The effects of ultrasonication on the physicochemical properties of bovine serum albumin (BSA)–glucose and the galactose conjugates formed by glycation was investigated. Fourier transform ion cyclotron resonance mass spectra analysis showed that the conjugates had a higher molecular weight than the native and ultrasonicated BSA. Ultrasonicated BSA had significantly higher emulsifying and foaming properties than native BSA. The browning intensity, surface hydrophobicity, emulsifying property and foaming capacity of the conjugates were substantially improved while the free amino groups, intrinsic fluorescence emission and foaming stability were decreased compared to native and ultrasonicated BSA. The results of this study indicate that ultrasonication is an efficient technique to improve the physicochemical properties of proteins. The glycation between ultrasonicated BSA and monosaccharide can effectively improve the physicochemical properties of BSA, and the glycation rate order is galactose \gt glucose. It also shows the critical role of monosaccharide conformational changes in improving the glycation and physicochemical properties of proteins.
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