AI Article Synopsis
- - The study focused on creating a conjugate of (-)-Epigallocatechin-3-gallate (EGCG) with whey protein isolate (WPI) using three different methods: alkaline treatment, free radical grafting, and enzyme-assisted oxidation.
- - Advanced techniques like Fourier transform infrared spectroscopy confirmed the successful linking of EGCG to WPI, with the enzyme method showing the highest efficiency in this process.
- - The resulting WPI-EGCG conjugates exhibited enhanced emulsifying and antioxidant properties, effectively stabilizing β-carotene emulsions by forming smaller droplets, and this effectiveness increased with higher EGCG content in the conjugates.
Article Abstract
(-)-Epigallocatechin-3-gallate (EGCG) was conjugated to whey protein isolate (WPI) using alkaline treatment, free radical grafting and tyrosinase-catalyzed oxidation. The structure and properties of the obtained conjugates and their application as antioxidant emulsifiers in stabilizing β-carotene emulsion were systematically characterized. Fourier transform infrared spectroscopy and sodium dodecyl sulfate-polyacrylamide gel electrophoresis verified the covalent linking between WPI and EGCG. The highest grafting efficiency was obtained for enzyme conjugate, followed for alkaline conjugate. Conjugation of EGCG decreased the α-helix content and fluorescence intensity of protein, and these changes depend on both EGCG conjugation and the cross-linking methods. Due to their improved emulsifying properties and antioxidant activity, WPI-EGCG conjugates formed smaller emulsion droplets and protect the encapsulated β-carotene more effectively, and the protective property is positively correlated with EGCG content in conjugates.
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| http://dx.doi.org/10.1016/j.foodchem.2022.133727 | DOI Listing |
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