| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6400947 | LWT - Food Science and Technology | 2016 | 6 Pages |
â¢Covalent modification by EGCG induced cross-linking on proteins of WPI.â¢The modification changed the conformational structures of proteins in WPI.â¢EGCG modification improved the foaming and emulsifying properties of WPI.
The physicochemical and functional properties of covalently modified whey protein isolate (WPI) by (â)-epigallocatechin-3-gallate (EGCG) were investigated. WPI was chemically modified by EGCG under alkaline conditions. The effect of modification on foaming and emulsifying properties was evaluated. The results of SDS-PAGE and size exclusion chromatography indicated that modification by EGCG induced cross-linking on proteins of WPI. Fourier transform infrared spectroscopy (FT-IR) analysis illustrated the incorporation of phenolic groups into the modified WPI and the changes in protein secondary structure. Intrinsic fluorescence spectra revealed that modified WPI had a more compact tertiary structure compared to unmodified WPI. The modified WPI exhibited better foaming and emulsifying properties than unmodified WPI. These results suggest that EGCG modification is a potential method for improving the functional properties of WPI.
