@article{AliHomannKhaliletal.2013, author = {Ali, Mostafa and Homann, Thomas and Khalil, Mahmoud and Kruse, Hans-Peter and Rawel, Harshadrai Manilal}, title = {Milk whey protein modification by coffee-specific phenolics effect on structural and functional properties}, series = {Journal of agricultural and food chemistry : a publication of the American Chemical Society}, volume = {61}, journal = {Journal of agricultural and food chemistry : a publication of the American Chemical Society}, number = {28}, publisher = {American Chemical Society}, address = {Washington}, issn = {0021-8561}, doi = {10.1021/jf402221m}, pages = {6911 -- 6920}, year = {2013}, abstract = {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 of this modification provides an innovative approach for functionalizing proteins and their uses in the food industry.}, language = {en} } @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} } @article{KhalilRailaAlietal.2012, author = {Khalil, Mahmoud and Raila, Jens and Ali, Mostafa and Islam, Khan M. S. and Schenk, Regina and Krause, Jens-Peter and Schweigert, Florian J. and Rawel, Harshadrai Manilal}, title = {Stability and bioavailability of lutein ester supplements from Tagetes flower prepared under food processing conditions}, series = {Journal of functional food}, volume = {4}, journal = {Journal of functional food}, number = {3}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1756-4646}, doi = {10.1016/j.jff.2012.03.006}, pages = {602 -- 610}, year = {2012}, abstract = {Tagetes spp. belongs to the Asteraceae family. It is recognized as a major source of lutein ester (lutein esterified with fatty acids such as lauric, myristic and palmitic acids), a natural colorant belonging to the xanthophylls or oxygenated carotenoids. Four species of Tagetes flower (Tagetes tenuifolia, Tagetes erecta, Tagetes patula, and Tagetes lucida) were used to extract lutein and lutein esters with three different methods. The results showed that T. erecta, type "orangeprinz", is the richest source of lutein esters (14.4 +/- 0.234 mg/g) in comparison to other Tagetes spp. No significant differences between extractions of lutein esters with medium-chain triacylglycerols (MCT) oil, orange oil or solvent (hexane/isopropanol) could be observed. MCT oil also improved stability of lutein esters at 100 degrees C for 40 min. Emulsification of MCT oil improved the stability of lutein ester extract against UV light at 365 nm for 72 h. Finally, an emulsion was prepared under food processing conditions, spray dried and its bioavailability investigated in a preliminary human intervention study. The results show a lower resorption, but further data suggest improvements in implementation of such supplements. (c) 2012 Elsevier Ltd. All rights reserved.}, language = {en} }