2019
DOI: 10.1039/c9ra07808h
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Recent advances in phenolic–protein conjugates: synthesis, characterization, biological activities and potential applications

Abstract: This review summarizes recent advances in the synthesis, characterization, biological activities and potential applications of phenolic–protein conjugates.

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Cited by 92 publications
(60 citation statements)
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References 96 publications
(88 reference statements)
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“…Moreover, the highest TPC was observed in ethanol fraction revealing that phenolic compounds bound to proteins were precipitated in this fraction. The antioxidant activity of protein fraction soluble in 70% ethanol could be highly increased by protein conjugation with phenolic compounds [ 54 ]. Antioxidant activity of phenolic–protein conjugates is effected by the amount of phenols covalently bounded to proteins and it is strongly related to the sort of phenolic compound attached [ 54 ].…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Moreover, the highest TPC was observed in ethanol fraction revealing that phenolic compounds bound to proteins were precipitated in this fraction. The antioxidant activity of protein fraction soluble in 70% ethanol could be highly increased by protein conjugation with phenolic compounds [ 54 ]. Antioxidant activity of phenolic–protein conjugates is effected by the amount of phenols covalently bounded to proteins and it is strongly related to the sort of phenolic compound attached [ 54 ].…”
Section: Resultsmentioning
confidence: 99%
“…The antioxidant activity of protein fraction soluble in 70% ethanol could be highly increased by protein conjugation with phenolic compounds [ 54 ]. Antioxidant activity of phenolic–protein conjugates is effected by the amount of phenols covalently bounded to proteins and it is strongly related to the sort of phenolic compound attached [ 54 ]. Nwachukwu and Aluko [ 55 ] noticed that differences in the peptide conformation which could also have contributed to the evaluation of antioxidant capacities.…”
Section: Resultsmentioning
confidence: 99%
“…The interaction often results in non-covalent binding of NH 2 groups of amino acids and OH groups of polyphenols. It was also reported that in some cases covalent adducts including Schiff bases can be formed [ 36 , 37 ].…”
Section: Introductionmentioning
confidence: 99%
“…It is important also to note that after oxidation, covalent interactions can form between the polyphenol degradation products and the protein, changing the protein's functional properties (Prigent, Voragen, Visser, van Koningsveld, & Gruppen, 2007). Furthermore, studies at relatively high pH did not confirm the lack of covalent bonds’ formation that is known to occur at alkaline conditions (Liu et al., 2019) and should be further verified. Although the affinity of polyphenol–protein interaction as a function of polyphenol structure is relatively well described, still a significantly larger gap exists regarding the impact of such interactions on polyphenols stability, especially for nonanthocyanin polyphenols.…”
Section: Effects Of Polyphenol–protein Interaction On the Stabilitymentioning
confidence: 89%