Exploration of the Stabilization Mechanism and Curcumin Bioaccessibility of Emulsions Stabilized by Whey Protein Hydrolysates after Succinylation and Glycation in Different Orders

March 24, 2020

Title

Exploration of the Stabilization Mechanism and Curcumin Bioaccessibility of Emulsions Stabilized by Whey Protein Hydrolysates after Succinylation and Glycation in Different Orders

Author

Yi Pan, Xiao-Min Li, Ran Meng, Bao Zhang

Year

2020

Journal

Journal of Agriculture and Food Chemistry

Abstract

The combined effects of succinic anhydride (SA) succinylation and linear dextrin (LD) glycation on whey protein hydrolysates (WPH) and their stabilized emulsions were evaluated. Degree of succinylation (DS), degree of glycation (DG), and degree of browning of samples suggested that a competitive displacement of reactive groups existed when WPH reacted with SA and LD in different orders. Attenuated total reflection Fourier transform infrared (ATR-FTIR) and far-UV circular dichroism (CD) indicated that the order of modification methods had a significant effect on secondary structures of WPH. Succinylation combined with glycation effectively reduced the surface hydrophobicity and increased the molecular flexibility of WPH. Meanwhile, the total free −SH content decreased, and the exposed free −SH content increased. Results of storage stability and gastrointestinal fate of the curcumin-loaded emulsion revealed that the modified WPH with higher DS was more effective for improving the curcumin bioaccessibility, while that with higher DG was more effective for enhancing the stability of the emulsion.

Instrument

J-810

Keywords

Circular dichroism, Secondary structure, Protein stability, Food science, Biochemistry