期刊
FOOD CHEMISTRY
卷 232, 期 -, 页码 744-752出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.04.074
关键词
Beta-lactoglobulin; Epigallocatechin-3-gallate; Glycation; Maillard reaction; Protein polyphenol interactions; Tea
资金
- GA of the Ministry of Education, Science and Technological Development of the Republic of Serbia [172024]
- FP7 RegPot project FCUB-ERA GA [256716]
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.
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