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Characterization and modeling of the interactions between coffee storage proteins and phenolic compounds

  • This study addresses the interactions of coffee storage proteins with coffee-specific phenolic compounds. Protein profiles, of Coffea arabica and Coffea canephora (var robusta) were compared. Major Phenolic compounds were extracted and analyzed with appropriate methods. The polyphenol-protein interactions during protein extraction have been addressed by different analytical setups [reversed-phase high-performance liquid chromatography (RP-HPLC), sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), matrix-assisted laser desorption ionization-time of flight-mass spectrometry (MALDI-TOF-MS), and Trolox equivalent antioxidant capacity (TEAC) assays], with focus directed toward identification of covalent adduct formation. The results indicate that C. arabica proteins are more susceptible to these interactions and the polyphenol oxidase activity seems to be a crucial factor for the formation of these addition products. A tentative allocation of the modification type and site in the protein has been attempted. Thus, theThis study addresses the interactions of coffee storage proteins with coffee-specific phenolic compounds. Protein profiles, of Coffea arabica and Coffea canephora (var robusta) were compared. Major Phenolic compounds were extracted and analyzed with appropriate methods. The polyphenol-protein interactions during protein extraction have been addressed by different analytical setups [reversed-phase high-performance liquid chromatography (RP-HPLC), sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), matrix-assisted laser desorption ionization-time of flight-mass spectrometry (MALDI-TOF-MS), and Trolox equivalent antioxidant capacity (TEAC) assays], with focus directed toward identification of covalent adduct formation. The results indicate that C. arabica proteins are more susceptible to these interactions and the polyphenol oxidase activity seems to be a crucial factor for the formation of these addition products. A tentative allocation of the modification type and site in the protein has been attempted. Thus, the first available in silico modeling of modified coffee proteins is reported. The extent of these modifications may contribute to the structure and function of "coffee melanoidins" and are discussed in the context of coffee flavor formation.show moreshow less

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Metadaten
Author:Mostafa Ali, Thomas Homann, Janka Kreisel, Mahmoud Khalil, Ralf Puhlmann, Hans-Peter Kruse, Harshadrai Rawel
DOI:https://doi.org/10.1021/jf303372a
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:2012
Year of Completion:2012
Release Date:2017/03/26
Tag:Coffee beans; antioxidants; modeling; phenolic compounds; protein-phenol interactions; storage proteins
Volume:60
Issue:46
Pagenumber:8
First Page:11601
Last Page:11608
Funder:Egyptian government
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie
Peer Review:Referiert