Background: Polyphenols have a strong binding capacity with proteins, but the binding behavior of polyphenols with glycosylated proteins and the effects of binding on the structure of glycosylated proteins have been less studied.
Results: This study used enzymatic modification to prepare an oligochitosan-legumin complex (OLC) to investigate its interaction with (-)-epigallocatechin gallate (EGCG) and quercetin. Fluorescence spectroscopy experiments showed that the binding site of OLC to EGCG was 27.7 ± 2.47 and that of quercetin to OLC was 19.5 ± 2.92; the binding of one polyphenol affected the other's ability to bind to OLC. The FTIR and CD results showed secondary structural changes in OLC after incorporating polyphenols, with a decrease in the content of α-helix and an increase in the content of β-sheet. The OLC and OLC-polyphenol complexes showed smaller particle size and denser micromorphology. Moreover, OLC had a protective effect on EGCG and quercetin against thermal and ultraviolet light treatments compared to polyphenols alone.
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The Journal of the Science of Food and Agriculture publishes peer-reviewed original research, reviews, mini-reviews, perspectives and spotlights in these areas, with particular emphasis on interdisciplinary studies at the agriculture/ food interface.
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