Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction
Authorized Users Only
Minić, Simeon L.
Article (Published version)
MetadataShow full item record
Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both ...glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved.
Keywords:Beta-lactoglobulin / Epigallocatechin-3-gallate / Glycation / Maillard reaction / Protein polyphenol interactions / Tea
Source:Food Chemistry, 2017, 232, 744-752
- Elsevier Sci Ltd, Oxford
- Molecular properties and modifications of some respiratory and nutritional allergens (RS-172024)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3027