TY - JOUR A1 - Kruse, Hans-Peter A1 - Heydenreich, Matthias A1 - Engst, W. A1 - Schilde, Uwe A1 - Kroll, Jürgen T1 - The identification of 1,3-oxazolidine-2-thiones and 1,3-thiazolidine-2-thiones from the reaction of glucose with benzyl isothiocyanate N2 - The structure of interaction products resulting from the reaction of unmodified glucose with benzyl isothiocyanate is reported. Prior to their identification, the main products of this reaction were isolated using solid- phase extraction (SPE) as well as preparative HPLC. They were then identified by NMR and MS as 3-benzyl-4-hydroxy-5-(D- arabino-1,2,3,4-tetrahydroxybutyl)- 1,3-oxazolidine-2-thione, 3-benzyl-4-hydroxy-4-hydroxymethyl-5-(D-erythro-1,2,3- trihydroxypropyl)- 1,3-oxazolidine-2-thione, N-benzyl-(D-gluco-4,5-dihydroxy-6-hydroxymethyl-tetrahydropyrano)[2,3-b] oxazolidine-2-thione and 3-benzyl-4-(N-benzyl amino)-5-(D-arabino-1,2,3,4-tetrahydroxybutyl)-1,3-thiazolidine-2-thione . The identity of the last compound was secured by X-ray crystal structure data. (C) 2004 Elsevier Ltd. All rights reserved Y1 - 2005 SN - 0008-6215 ER - TY - JOUR A1 - Rawel, Harshadrai Manilal A1 - Rohn, Sascha A1 - Kruse, Hans-Peter A1 - Kroll, Jürgen T1 - Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid N2 - Bovine serum albumin (BSA) was modifed by covalent attachment of chlorogenic acid using different concentrations at pH 9. The derivatization was accompanied by a reduction of lysine, cysteine and tryptophan residues. The isoelectric points were shifted to lower pH values and formation of high molecular weight fractions was noted. The structural changes were studied using circular dichroism, differential scanning calorimetry (DSC), intrinsic fluorescence, and binding of anilinonaphthalenesulfonic acid. The results showed that the content of alpha-helix decreased with a parallel increase in unordered structures with higher degrees of derivatization. DSC revealed a decrease in both denaturation temperature and enthalpy. Surface hydrophobicity declined, indicating that hydrophilic regions were exposed on the molecular surface. Proteolytic digestion showed that, at a lower degree of derivatization,the tryptic degradation was most adversely effected, whereas the peptic digestion declined with increasing modification. A trypsin inhibitory effect of the breakdown products released from derivatized BSA was also observed. Y1 - 2002 ER - TY - JOUR A1 - Stoof, Gisela A1 - Kruse, Hans-Peter A1 - Anger, Horst T1 - Hydrothermische Behandlung von Stärke in Gegenwart von -Amylase Y1 - 1994 ER - TY - JOUR A1 - Stoof, Gisela A1 - Anger, Horst A1 - Kruse, Hans-Peter T1 - The yield of resistant starch after hydrothermal treatment Y1 - 1994 ER - TY - JOUR A1 - Kruse, Hans-Peter A1 - Kroll, Jürgen T1 - Fettaustauscher : lebensmittelchemische und ernährungsphysiologische Aspekte Y1 - 1995 ER - TY - JOUR A1 - Eggert, Kai A1 - Hollmann, Juergen A1 - Hiller, Beate A1 - Kruse, Hans-Peter A1 - Rawel, Harshadrai Manilal A1 - Pawelzik, Elke T1 - Effects of Fusarium infection on the phenolics in emmer and naked barley N2 - Inoculated or non-inoculated naked barley and emmer cultivars were investigated with regard to their influence on phenolic acid profiles and their arabinoxylan content. Two groups of phenolic compounds were differentiated-methanol- soluble and hydrolyzable covalent-bound phenolic compounds. Chromatographic methods were applied for their analysis. The results showed ferulic acid as the predominant phenol in both total and covalent-bound fractions. The inoculation significantly reduced the ferulic acid content within a range of 5.6-6.6% in the two cereals and all their cultivars. Naked barley cultivars additionally contained the flavonoid catechin in the soluble fraction. The innoculation led here to a significant increase in the catechin content of about 4.5%. These results document an induction of the synthesis of catechin in naked barley after artificial Fusarium infection, whereas the ferulic acid content declined. Y1 - 2010 UR - http://pubs.acs.org/journal/jafcau U6 - https://doi.org/10.1021/Jf903545j SN - 0021-8561 ER - TY - JOUR A1 - Kruse, Hans-Peter A1 - Stoof, Gisela A1 - Rubbert, Helga A1 - Anger, Horst T1 - Characterisation of fat replacers Y1 - 1994 ER - TY - JOUR A1 - Kruse, Hans-Peter T1 - Bewertung des Sättigungsempfindens mittels Fuzzy-Logik Y1 - 1996 ER - TY - JOUR A1 - Ali, Mostafa A1 - Homann, Thomas A1 - Khalil, Mahmoud A1 - Kruse, Hans-Peter A1 - Rawel, Harshadrai Manilal T1 - Milk whey protein modification by coffee-specific phenolics effect on structural and functional properties JF - Journal of agricultural and food chemistry : a publication of the American Chemical Society N2 - 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. KW - coffee phenolic compounds KW - whey proteins KW - antioxidants KW - protein-phenol interactions KW - modeling KW - functionalizing proteins Y1 - 2013 U6 - https://doi.org/10.1021/jf402221m SN - 0021-8561 VL - 61 IS - 28 SP - 6911 EP - 6920 PB - American Chemical Society CY - Washington ER - TY - JOUR A1 - Ali, Mostafa A1 - Homann, Thomas A1 - Kreisel, Janka A1 - Khalil, Mahmoud A1 - Puhlmann, Ralf A1 - Kruse, Hans-Peter A1 - Rawel, Harshadrai Manilal T1 - Characterization and modeling of the interactions between coffee storage proteins and phenolic compounds JF - Journal of agricultural and food chemistry : a publication of the American Chemical Society N2 - 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. KW - Coffee beans KW - storage proteins KW - phenolic compounds KW - antioxidants KW - protein-phenol interactions KW - modeling Y1 - 2012 U6 - https://doi.org/10.1021/jf303372a SN - 0021-8561 VL - 60 IS - 46 SP - 11601 EP - 11608 PB - American Chemical Society CY - Washington ER -