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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.show moreshow less

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Metadaten
Author:Mostafa Ali, Thomas Homann, Mahmoud Khalil, Hans-Peter Kruse, Harshadrai Rawel
DOI:https://doi.org/10.1021/jf402221m
ISSN:0021-8561 (print)
Parent Title (English):Journal of agricultural and food chemistry : a publication of the American Chemical Society
Publisher:American Chemical Society
Place of publication:Washington
Document Type:Article
Language:English
Year of first Publication:2013
Year of Completion:2013
Release Date:2017/03/26
Tag:antioxidants; coffee phenolic compounds; functionalizing proteins; modeling; protein-phenol interactions; whey proteins
Volume:61
Issue:28
Pagenumber:10
First Page:6911
Last Page:6920
Funder:Egyptian government of the Ph.D students
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie
Peer Review:Referiert