@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{EggertHollmannHilleretal.2010, author = {Eggert, Kai and Hollmann, Juergen and Hiller, Beate and Kruse, Hans-Peter and Rawel, Harshadrai Manilal and Pawelzik, Elke}, title = {Effects of Fusarium infection on the phenolics in emmer and naked barley}, issn = {0021-8561}, doi = {10.1021/Jf903545j}, year = {2010}, abstract = {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.}, language = {en} } @article{Kruse1996, author = {Kruse, Hans-Peter}, title = {Bewertung des S{\"a}ttigungsempfindens mittels Fuzzy-Logik}, year = {1996}, language = {de} } @article{Kruse2001, author = {Kruse, Hans-Peter}, title = {Can satiety be measured?}, year = {2001}, abstract = {An energy-controlled study on a Western diet composed of 45\% fat, 40\% carbohydrate and 15\% protein by energy was carried out. The study consisted of four test phases having a length of 9 days in each case, where 8 healthy free- living subjects were adjusted to individual energy requirements at maintenance level. Between the tests, wash-out phases of 4-5 months were inserted to avoid adaptation effects. By using a standard breakfast of constant composition, satiety was evaluated by applying the concept of categorical comparison, which was based on the common fact, that the perception between two meals is changed and usually a set of sensations can be discriminated. These were termed very full and full (just after finishing a meal), appetite and hungry (just before the next meal). These sensations were used as categories on a categorical scale. The evaluation of satiety was performed such that on each day of the four test phases the subjects had to select over a period of 4 h every 30 min one category out of the four, what corresponded to the individual sensation at that time. This procedure was followed by a mathematical treatment of data such that the individual judgements were transformed into a numerical system. As a result, the time course of satiety was available characterizing the time-dependent change of the interoception after consuming the test meal. Using this concept highly reliable results were obtained as demonstrated by the comparison of the four test series.}, language = {en} } @article{KruseHeydenreichEngstetal.2005, author = {Kruse, Hans-Peter and Heydenreich, Matthias and Engst, W. and Schilde, Uwe and Kroll, J{\"u}rgen}, title = {The identification of 1,3-oxazolidine-2-thiones and 1,3-thiazolidine-2-thiones from the reaction of glucose with benzyl isothiocyanate}, issn = {0008-6215}, year = {2005}, abstract = {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}, language = {en} } @article{KruseKlessenBlaut1999, author = {Kruse, Hans-Peter and Klessen, Brigitta and Blaut, Michael}, title = {Effects of inulin of faecal bifidobateria in human subjects}, year = {1999}, language = {en} } @article{KruseKroll1995, author = {Kruse, Hans-Peter and Kroll, J{\"u}rgen}, title = {Fettaustauscher : lebensmittelchemische und ern{\"a}hrungsphysiologische Aspekte}, year = {1995}, language = {de} } @article{KruseStoofRubbertetal.1994, author = {Kruse, Hans-Peter and Stoof, Gisela and Rubbert, Helga and Anger, Horst}, title = {Characterisation of fat replacers}, year = {1994}, language = {en} } @article{RawelRohnKruseetal.2002, author = {Rawel, Harshadrai Manilal and Rohn, Sascha and Kruse, Hans-Peter and Kroll, J{\"u}rgen}, title = {Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid}, year = {2002}, abstract = {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.}, language = {en} }