@article{AliHomannKreiseletal.2012,
  author    = {Ali, Mostafa and Homann, Thomas and Kreisel, Janka and Khalil, Mahmoud and Puhlmann, Ralf and Kruse, Hans-Peter and Rawel, Harshadrai Manilal},
  title     = {Characterization and modeling of the interactions between coffee storage proteins and phenolic compounds},
  series = {Journal of agricultural and food chemistry : a publication of the American Chemical Society},
  volume    = {60},
  journal   = {Journal of agricultural and food chemistry : a publication of the American Chemical Society},
  number    = {46},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0021-8561},
  doi       = {10.1021/jf303372a},
  pages     = {11601 -- 11608},
  year      = {2012},
  abstract  = {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, 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.},
  language  = {en}
}