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The Effect of (−)-Epigallocatechin-3-Gallate Non-Covalent Interaction with the Glycosylated Protein on the Emulsion Property.
- Source :
-
Polymers (20734360) . Oct2019, Vol. 11 Issue 10, p1688-1688. 1p. 1 Diagram, 2 Charts, 4 Graphs. - Publication Year :
- 2019
-
Abstract
- The effect of (−)-epigallocatechin-3-gallate (EGCG) on protein structure and emulsion properties of glycosylated black bean protein isolate (BBPI-G) were studied and compared to native black bean protein isolate (BBPI). The binding affinity of BBPI and BBPI-G with EGCG belonged to non-covalent interaction, which was determined by fluorescence quenching. EGCG attachment caused more disordered protein conformation, leading to a higher emulsification property. Among the different EGCG concentrations (0.10, 0.25, 0.50 mg/mL), the result revealed that the highest level of the emulsification property was obtained with 0.25 mg/mL EGCG. Therefore, the BBPI-EGCG and BBPI-G-EGCG prepared by 0.25 mg/mL EGCG were selected to fabricate oil-in-water (O/W) emulsions. After the addition of EGCG, the mean particle size of emulsions decreased with the increasing absolute value of zeta-potential, and more compact interfacial film was formed due to the higher percentage of interfacial protein adsorption (AP%). Meanwhile, EGCG also significantly reduced the lipid oxidation of emulsions. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 20734360
- Volume :
- 11
- Issue :
- 10
- Database :
- Academic Search Index
- Journal :
- Polymers (20734360)
- Publication Type :
- Academic Journal
- Accession number :
- 139604597
- Full Text :
- https://doi.org/10.3390/polym11101688