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Milk whey protein modification by coffee-specific phenolics effect on structural and functional properties

  • A suitable vehicle for integration of bioactive plant constituents is proposed. It involves modification of proteins using phenolics and applying these for protection of labile constituents. It dissects the noncovalent and covalent interactions of beta-lactoglobulin with coffee-specific phenolics. Alkaline and polyphenol oxidase modulated covalent reactions were compared. Tryptic digestion combined with MALDI-TOF-MS provided tentative allocation of the modification type and site in the protein, and an in silico modeling of modified beta-lactoglobulin is proposed. The modification delivers proteins with enhanced antioxidative properties. Changed structural properties and differences in solubility, surface hydrophobicity, and emulsification were observed. The polyphenol oxidase modulated reaction provides a modified beta-lactoglobulin with a high antioxidative power, is thermally more stable, requires less energy to unfold, and, when emulsified with lutein esters, exhibits their higher stability against UV light. Thus, adaptation ofA suitable vehicle for integration of bioactive plant constituents is proposed. It involves modification of proteins using phenolics and applying these for protection of labile constituents. It dissects the noncovalent and covalent interactions of beta-lactoglobulin with coffee-specific phenolics. Alkaline and polyphenol oxidase modulated covalent reactions were compared. Tryptic digestion combined with MALDI-TOF-MS provided tentative allocation of the modification type and site in the protein, and an in silico modeling of modified beta-lactoglobulin is proposed. The modification delivers proteins with enhanced antioxidative properties. Changed structural properties and differences in solubility, surface hydrophobicity, and emulsification were observed. The polyphenol oxidase modulated reaction provides a modified beta-lactoglobulin with a high antioxidative power, is thermally more stable, requires less energy to unfold, and, when emulsified with lutein esters, exhibits their higher stability against UV light. Thus, adaptation of this modification provides an innovative approach for functionalizing proteins and their uses in the food industry.zeige mehrzeige weniger

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Metadaten
Verfasserangaben:Mostafa Ali, Thomas HomannORCiD, Mahmoud Khalil, Hans-Peter Kruse, Harshadrai Manilal RawelORCiDGND
DOI:https://doi.org/10.1021/jf402221m
ISSN:0021-8561
Titel des übergeordneten Werks (Englisch):Journal of agricultural and food chemistry : a publication of the American Chemical Society
Verlag:American Chemical Society
Verlagsort:Washington
Publikationstyp:Wissenschaftlicher Artikel
Sprache:Englisch
Jahr der Erstveröffentlichung:2013
Erscheinungsjahr:2013
Datum der Freischaltung:26.03.2017
Freies Schlagwort / Tag:antioxidants; coffee phenolic compounds; functionalizing proteins; modeling; protein-phenol interactions; whey proteins
Band:61
Ausgabe:28
Seitenanzahl:10
Erste Seite:6911
Letzte Seite:6920
Fördernde Institution:Egyptian government of the Ph.D students
Organisationseinheiten:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie
Peer Review:Referiert
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