2015
DOI: 10.1016/j.foodhyd.2014.05.022
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Glycosylation of bovine serum albumin via Maillard reaction prevents epigallocatechin-3-gallate-induced protein aggregation

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Cited by 50 publications
(47 citation statements)
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“…The same inhibitory mechanism was described for the polyphenol family by Bhattacherjee and Datta [31]. In their study, they found syringic acid to a better AGE inhibitor than chlorogenic acid because it is a smaller molecule and therefore has higher accessibility to bind to amino groups of lysine [32]. Therefore, syringic acid is also a competitive inhibitor of glucose.…”
Section: Resultssupporting
confidence: 53%
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“…The same inhibitory mechanism was described for the polyphenol family by Bhattacherjee and Datta [31]. In their study, they found syringic acid to a better AGE inhibitor than chlorogenic acid because it is a smaller molecule and therefore has higher accessibility to bind to amino groups of lysine [32]. Therefore, syringic acid is also a competitive inhibitor of glucose.…”
Section: Resultssupporting
confidence: 53%
“…Therefore, syringic acid is also a competitive inhibitor of glucose. Another study described high aggregation inhibition and AGE formation with epigallocatechin-3-gallate [32]. This is mainly due to the building of stable colloid between epigallocatechin-3-gallate and albumin, which may protect against any other intermolecular interactions [32].…”
Section: Resultsmentioning
confidence: 99%
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“…Maillard reaction is a nontoxic natural reaction, which conjugates proteins and polysaccharides by linking the carbonyl group of polysaccharides to the unprotonated amino group of proteins under controlled conditions. Different proteins such as casein, [19][20][21] lysozyme, [22] bovine serum albumin,- [23,24] and soybean protein [25] were reported to conjugate with polysaccharides, giving significantly increased solubility, stability, and other functional properties such as emulsifying ability. Proteinpolysaccharide conjugates can self-assemble into micelles with a hydrophobic protein core and a hydrophilic polysaccharide shell.…”
Section: Introductionmentioning
confidence: 99%
“…Proteinpolysaccharide conjugates can self-assemble into micelles with a hydrophobic protein core and a hydrophilic polysaccharide shell. The micelles of protein-polysaccharide conjugates were previously used to encapsulate hydrophobic compounds such as pyrene, [19] β-carotene, [26] and tea catechin.- [21,24,27] However, few work has been reported to use protein-polysaccharide conjugate micelles as the carrier for hydrophobic curcumin so far.…”
Section: Introductionmentioning
confidence: 99%