2013
DOI: 10.1016/j.foodres.2013.05.033
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Interactions of black and green tea polyphenols with whole milk

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Cited by 116 publications
(67 citation statements)
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“…The secondary structure of BSA is known to be mostly composed of α-helices of nine helical loops connected with 17 disulfide bridges. The α-helix value in buffer solution is in good agreement with those previously reported [62][63][64]. The α-helix content of BSA in the studied protein stabilizers is given in Table 2.…”
Section: Protein Stabilitysupporting
confidence: 89%
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“…The secondary structure of BSA is known to be mostly composed of α-helices of nine helical loops connected with 17 disulfide bridges. The α-helix value in buffer solution is in good agreement with those previously reported [62][63][64]. The α-helix content of BSA in the studied protein stabilizers is given in Table 2.…”
Section: Protein Stabilitysupporting
confidence: 89%
“…S6 in the Supporting Information)) to determine the BSA secondary structure. In the buffer solution, the bands at (1615, 1631, 1653, 1675, and 1697) cm -1 are assigned to intermolecular β-sheet, intramolecular β-sheet, α-helix, turn, and antiparallel β-sheet, respectively [62][63][64]. The secondary structure of BSA is known to be mostly composed of α-helices of nine helical loops connected with 17 disulfide bridges.…”
Section: Protein Stabilitymentioning
confidence: 99%
“…Casein milk has a stronger affinity binding to tea polyphenols than whey proteins [4,5,8] Tea polyphenols have the ability to interact with milk proteins especially proline-rich proteins such as casein. The proline group in casein protein has a strong affinity for the hydroxyl groups in polyphenols, since casein has the greatest effect on the decrease in tea antioxidant activity than other proteins in milk [4,5,6,11] Decreased antioxidant activity in tea mixes with milk because interaction between casein and polyphenol resulting in decreased tea antioxidant activity while the distilled water in the control solution did not bind to polyphenols so decreased antioxidant activity in the control solution due dilution effect by the distilled water [14,15,17]. The affinity of polyphenol bonds to proteins depends on the size of the polyphenol molecule, meaning the stronger the affinity for larger molecules of polyphenols.…”
Section: Fig2 Stable Free Radical Diphenylpicrylhydrazyl (Dpph)mentioning
confidence: 99%
“…Polyphenols with larger molecules such as theaflavin in black tea are easier to form complex and bind to proteins. The bond will reduce the number of available hydroxyl groups and reduce the capacity of polyphenol electron donors thereby decreasing greater antioxidant activity in black tea than white tea [10,13,15,17]. Black tea processing takes place oxidation by polyphenol oxidase enzymes that convert catechins into theaflavins and thearubigins that have large polyphenol structures so that black tea has a lower catechinmore than green tea content and theaflavin and tearubigine higher [13,18].…”
Section: Fig2 Stable Free Radical Diphenylpicrylhydrazyl (Dpph)mentioning
confidence: 99%
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