@article{HernandezTrianaKrollProlletal.1996, author = {Hernandez-Triana, Manuel and Kroll, J{\"u}rgen and Proll, J{\"u}rgen and Noack, Jutta and Petzke, Klaus-J{\"u}rgen}, title = {Benzyl-isothiocyanate (BITC) decreases quality of egg white proteins in rats}, year = {1996}, language = {en} } @article{RohnPetzkeRaweletal.2006, author = {Rohn, Sascha and Petzke, Klaus-J{\"u}rgen and Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen}, title = {Reactions of chlorogenic acid and quercetin with a soy protein isolate - Influence on the in vivo food protein quality in rats}, series = {Molecular nutrition \& food research : bioactivity, chemistry, immunology, microbiology, safety, technology}, volume = {50}, journal = {Molecular nutrition \& food research : bioactivity, chemistry, immunology, microbiology, safety, technology}, publisher = {Wiley}, address = {Weinheim}, issn = {1613-4125}, doi = {10.1002/mnfr.200600043}, pages = {696 -- 704}, year = {2006}, abstract = {Plant phenolic compounds are known to interact with proteins producing changes in the food (e.g., biological value (BV), color, taste). Therefore, the in vivo relevance, especially, of covalent phenolprotein reactions on protein quality was studied in a rat bioassay. The rats were fed protein derivatives at a 10\% protein level. Soy proteins were derivatized with chlorogenic acid and quercetin (derivatization levels: 0.056 and 0.28 mmol phenolic compound/gram protein). Analysis of nitrogen in diets, urine, and fecal samples as well as the distribution of amino acids were determined. Depending on the degree of derivatization, the rats fed with soy protein derivatives showed an increased excretion of fecal and urinary nitrogen. As a result, true nitrogen digestibility, BV, and net protein utilization were adversely affected. Protein digestibility corrected amino acid score was decreased for lysine, tryptophan, and sulfur containing amino acids.}, language = {en} } @article{PetzkeSchuppeRohnetal.2005, author = {Petzke, Klaus-J{\"u}rgen and Schuppe, S. and Rohn, Sascha and Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen}, title = {Chlorogenic acid moderately decreases the quality of whey proteins in rats}, issn = {0021-8561}, year = {2005}, abstract = {During processing and storage, phenolic compounds (PCs) may react with food protein bound amino acids (AAs). Such reactions have been reported to change physicochemical and to decrease in vitro digestion properties of proteins. A rat growth and nitrogen (N) balance study was conducted to prove whether derivatization with chlorogenic acid (CA) affects the nutritional quality of beta-lactoglobulin (beta-LG). Test diets (10\% protein level) contained nonderivatized beta-LG (LG, treated under omission of CA), low derivatization level beta-LG (LGL), high derivatization level beta-LG (LGH), or casein supplemented with L-methionine (0.3\% of diet; C+met) as an internal standard. An additional group received untreated beta-LG supplemented with pure CA (1.03\% of diet; LG+CA). The AA composition of test proteins, plasma AAs, and liver glutathione (GSH) concentrations were determined. Protein digestibility-corrected amino acid score (PDCAAS) was calculated using human or rat AA requirement patterns and rat fecal digestibility values. N excretion was significantly higher in feces and lower in urine of rats fed with LGH as compared to LG and LGL. Consequently, true N digestibility (TND) was significantly lower with LGH as compared to LG and LGL. The lower content of methionine, cysteine, lysine, and tryptophan in LGH corresponded to a reduced TND. Net protein utilization (NPU) was not different between treated beta-LG fed diet groups but was lower than in LG+CA and C+met fed groups. Only at a relatively high level of derivatization with CA, the otherwise good nutritional quality of beta-LG is affected so that TND is reduced, while NPU still remains unaffected. Derivatization of beta-LG with CA does not seem to lead to an additional deficiency in a specific indispensable AA in growing rats fed with 10\% protein}, language = {en} } @article{KrollNoackRaweletal.1994, author = {Kroll, J{\"u}rgen and Noack, Jutta and Rawel, Harshadrai Manilal and Kr{\"o}ck, Regina and Proll, J{\"u}rgen}, title = {Chemical reactions of benzyl isothio cyanate with egg-white protein fractions}, year = {1994}, language = {en} } @article{KrollRawelKroecketal.1994, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal and Kr{\"o}ck, Regina and Proll, J{\"u}rgen and Schnaak, W.}, title = {Interactions of Isothiocyanates with egg white proteins}, year = {1994}, language = {en} } @article{RawelFreyMeidtneretal.2006, author = {Rawel, Harshadrai Manilal and Frey, Simone K. and Meidtner, Karina and Kroll, J{\"u}rgen and Schweigert, Florian J.}, title = {Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence}, series = {Molecular nutrition \& food research : bioactivity, chemistry, immunology, microbiology, safety, technology}, volume = {50}, journal = {Molecular nutrition \& food research : bioactivity, chemistry, immunology, microbiology, safety, technology}, number = {8}, publisher = {Wiley}, address = {Weinheim}, issn = {1613-4125}, doi = {10.1002/mnfr.200600013}, pages = {705 -- 713}, year = {2006}, abstract = {The noncovalent binding of selected phenolic compounds (chlorogenic-, ferutic-, gallic acid, quercetin, rutin, and isoquercetin) to proteins (HSA, BSA, soy glycinin, and lysozyme) was studied by an indirect method applying the quenching of intrinsic tryptophan fluorescence. From the data obtained, the binding constants were calculated by nonlinear regression (one site binding; y = Bx/k + x). It has been reported that tannins inhibit human salivary amylase and that these complexes may reduce the development of cariogenic plaques. Further, amylase contains two tryptophan residues in its active site. Therefore, in a second part of the study involving 31 human subjects, evidence was sought for noncovalent interactions between the phenols of green tea and saliva proteins as measured by the fluorescence intensity. Amylase activity was determined before and after the addition of green tea to saliva of 31 subjects. Forty percent of the subjects showed an increase in amylase activity contrary to studies reporting only a decrease in activity. The interactions of tannin with amylase result in a decrease of its activity. It still remains to be elucidated why amylase does not react uniformly under conditions of applying green tea to saliva. Further, in terms of using phenols as caries inhibitors this finding should be of importance.}, language = {en} } @article{EggertRawelNikfardjametal.2006, author = {Eggert, Kai and Rawel, Harshadrai Manilal and Nikfardjam, Martin S. Pour and Kroll, J{\"u}rgen}, title = {Interactions between lysozyme and wine components}, series = {Deutsche Lebensmittel-Rundschau : DLR}, volume = {102}, journal = {Deutsche Lebensmittel-Rundschau : DLR}, number = {10}, publisher = {Behr}, address = {Stuttgart}, issn = {0012-0413}, pages = {472 -- 478}, year = {2006}, abstract = {The addition of lysozyme amounting to 1000 mg/l wine does neither effect its total phenol content (Folin-Ciocalteu-Method), nor wine colour (measured by extinction at 512 nm) nor its antioxidative capacity (TEAC-Assay). No covalent binding of wine phenols to the enzyme was observed during lysozyme addition, although non-covalent interactions are possible. Lysozyme activity is not influenced by the presence of malvidin-3-glucoside and resveratrol in model experiments, whereas pH and ethanol content produce a corresponding alteration in lysozyme activity. With regard to red wine, a significant effect was noted in the presence of wine components.}, language = {de} } @article{RohnRawelRoberetal.2005, author = {Rohn, Sascha and Rawel, Harshadrai Manilal and Rober, M. and Kroll, J{\"u}rgen}, title = {Reactions with phenolic substances can induce changes in some physico-chemical properties and activities of bromelain - the consequences for supplementary food products}, issn = {0950-5423}, year = {2005}, abstract = {Bromelain was allowed to react with phenolic compounds. The activity and selected physico-chemical properties of the resulting derivatives were characterized. In vitro experiments showed that the proteolytic activity of bromelain was inhibited. Bromelain also serves as a food protein, because food stuffs based on pineapple contain relatively high concentrations of bromelain. In vitro digestion of bromelain derivatives with the main proteolytic enzymes of the gastrointestinal tract was also adversely affected. A covalent attachment of the phenolic compounds was identified at the tryptophan, free amino (lysines and N-terminal) and thiol groups of bromelain. A decrease in solubility of the derivatives was observed. The isoelectric point was shifted to lower pH values and high molecular weight fractions were identified. All effects observed depended on the reactivity of the phenolic substances. Two supplementary food products containing both bromelain and quercetin were also tested in terms of their proteolytic activity and digestibility}, language = {en} } @article{RawelRohnKroll2005, author = {Rawel, Harshadrai Manilal and Rohn, Sascha and Kroll, J{\"u}rgen}, title = {Characterisation of 11S protein fractions and phenolic compounds from green coffee beans under special consideration of their interactions - A review}, issn = {0012-0413}, year = {2005}, abstract = {The intention of this study was to increase the knowledge on the composition and structure of coffee bean proteins and the changes induced in them especially with regard to their interactions with the phenolic compounds also present. For this purpose green coffee beans were extracted by means of standard methanol extraction to quantify the chlorogenic acid content. Different solubilisation buffers were applied to extract the protein fractions with or without prior fat removal. The protein samples thus obtained were analysed by different methods (RP-HPLC, SDS-PAGE and SELDI-TOF- MS). Preliminary model studies were performed to characterize the interactions between the isolated green coffee protein fractions and chlorogenic acid (the major phenolic compound in coffee beans) with the intention of fulfilling the ultimate goal of characterizing such reactions in roasted coffee. The results show that the content of chlorogenic bound covalently to the protein increases. A reaction with the nucleophilic protein side chains (tryptophan, cystein and lysine) was recorded. Cross-inked protein polymers were also detected, whereby the a-chain was found to be more reactive. These reactions effect the solubility of the coffee bean proteins, the latter in turn becoming more acidic in nature. The secondary structure was affected only slightly as determined by circular dichroism. The in-vitro tryptic digestibility was also influenced, where again the cc-chain seems to be more susceptible. The observed polymerisation due to derivatisation by chorogenic acid declines the digestion. Similar digestion behaviour was also observed during tryptic hydrolysis of roasted coffee compared to that of green coffee, roasting allowing more stronger denaturation caused by the accompanying Maillard reaction. The derivatised green coffee bean proteins were found to have moderate antioxidative capacity}, language = {en} } @article{RawelMeidtnerKroll2005, author = {Rawel, Harshadrai Manilal and Meidtner, Karina and Kroll, J{\"u}rgen}, title = {Binding of selected phenolic compounds to proteins}, issn = {0021-8561}, year = {2005}, abstract = {In the context of this study, the noncovalent binding of selected phenolic compounds (chlorogenic, ferulic, and gallic acids, quercetin, rutin, and isocluercetin) to different proteins (human serum albumin, bovine serum albumin, soy glycinin, and lysozyme) was studied with direct (Hummel- Dreyer/size exclusion chromatography) and/or indirect methods (fluorescence absorbance properties of the binding components). In the latter case, the measurement of the phenol binding was achieved by exploiting the intrinsic fluorescence emission properties of cluercetin as a probe. From the data obtained, the binding constants and the number of binding sites were calculated. The binding parameters were influenced by different factors, where, e.g., increasing temperature and ionic strength as well as decreasing pH cause a diminished binding. The structures of the proteins as determined by circular dichroism indicate changes in the tertiary structure with the secondary structure remaining intact}, language = {en} } @article{KrollRantersRaweletal.2004, author = {Kroll, J{\"u}rgen and Ranters, Holger and Rawel, Harshadrai Manilal and Rohn, Sascha}, title = {Isoflavones as constituents of plant foods : Isoflavone als Bestandteile pflanzlicher Lebensmittel}, year = {2004}, abstract = {Vor dem Hintergrund der Diskussion {\"u}ber die ern{\"a}hrungsphysiologische Bedeutung von Isoflavonen befasst sich die vorliegende {\"U}bersichtsarbeit auf der Basis von 186 Literaturquellen mit der Struktur, dem Vorkommen, der Aufnahme, der Biosynthese, der Resorption, dem Metabolismus und der biologischen Wirkung dieser Untergruppen der Pflanzenphenole. Diskutiert werden sowohl positive als auch negative biologische Wirkungen dieser Verbindungen. Strukturabh{\"a}ngig k{\"o}nnen die Isoflavone mit anderen Lebensmittelinhaltsstoffen in Wechselwirkung treten. With the background of the actual ongoing discussion on the nutritional}, language = {de} } @article{RawelRohnKrolletal.2005, author = {Rawel, Harshadrai Manilal and Rohn, Sascha and Kroll, J{\"u}rgen and Schweigert, Florian J.}, title = {Surface enhanced laser desorptions ionization-time of flight-mass spectrometry analysis in complex food and biological systems}, year = {2005}, 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{RohnRawelKroll2004, author = {Rohn, Sascha and Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen}, title = {Antioxidant activity of protein-bound quercetin}, year = {2004}, abstract = {Bovine serum albumin (BSA) was derivatized by covalent attachment of different amounts of quercetin (ratios of BSA : quercetin were 20:1, 10:1, 7:1, 5:1, 2:1 (w/w)). The antioxidant activity of the protein-phenol derivatives was investigated using a modified TEAC assay. The results show that the covalent attachment of quercetin to BSA decreases the total antioxidant activity in comparison to an equivalent amount of free quercetin depending on the degree of derivatization. The derivative with the highest amount of covalently bound quercetin (2:1 derivative) showed an antioxidant activity of only 79\% compared to an equivalent amount of free quercetin. After the enzymatic proteolysis of the BSA quercetin derivatives with trypsin, the total antioxidant activity of the degradation products increases in comparison to the respective undigested derivatives, but does not reach the activity of an equivalent amount of free quercetin. Even after 240 minutes of tryptic degradation there is still a lack in antioxidant activity (for the 7:1 derivative nearly 33\%) as compared to free quercetin.}, language = {en} } @article{RawelRantersRohnetal.2004, author = {Rawel, Harshadrai Manilal and Ranters, Holger and Rohn, Sascha and Kroll, J{\"u}rgen}, title = {Assessment of the reactivity of selected isoflavones against proteins in comparison to quercetin}, year = {2004}, abstract = {Selected isoflavones (genistein, daidzein, formononetin, prunetin, biochanin A and two synthetic isoflavones) were allowed to interact with soy and whey proteins. The reaction products were analyzed in terms of covalent binding at the nucleophilic side chains of proteins. Changes in molecular properties of the proteins derivatives were documented by SDS-PAGE, IEF and SELDI-TOF-MS. The structural changes induced were studied using circular dichroism (CD). The in vitro digestibility was assessed with trypsin. The results show that the occurrence of the catechol moiety, i.e. the two adjacent (ortho) aromatic hydroxyl groups on ring B of the flavonoid structural skeleton appears to be perquisite condition for covalent binding to proteins. The catechol moiety on ring A was less reactive. Its absence lead to a slight or no significant reaction, although non-covalent interactions may still be possible even when lacking this structural element. A comparison of the data is also made with quercetin representing the flavonols.}, language = {en} } @article{KrollRohnRawel2004, author = {Kroll, J{\"u}rgen and Rohn, Sascha and Rawel, Harshadrai Manilal}, title = {Einsatz von MALDI- und SELDI-Massenspectrometrie zur Charakterisierung ausgew{\"a}hlten Nahrungsproteine und Proteinmodifikationen}, issn = {0250-1554}, year = {2004}, abstract = {The application of mass spectrometry for the characterization of food proteins represents one of the most important tools in food chemistry and nutritional science. In the last few years there has been a tremendous development in the classical questions with regard to determination of molecular mass, identification amino acid sequence and structure of proteins. With these technical improvements, it is becoming more and more interesting to characterize the changes involved in proteins embedded in the food matrix as a result of their technological processing, especially in terms of the influence on their functional, nutritional and phsiological properties. Many such posttransational protein modifications occuring due to reactions with other food constituents (e.g. secondary plant metabolites) provide a series of possible fields for application of a sample preparation with a soft ionisation technique using mass spectrometry. The matrix assisted laser desorptions/ionisation ? time of flight ? mass spectrometry (MALDI-TOF-MS) and the surface enhanced laser desorptions/ionisation ? time of flight ? mass spectrometry (SELDI-TOF-MS) have become since than two of the most important methods of choice for solving of such questions and these both techniques have been described here with correponding examples.}, language = {de} } @article{KrollRohnRawel2003, author = {Kroll, J{\"u}rgen and Rohn, Sascha and Rawel, Harshadrai Manilal}, title = {Sekund{\"a}re Inhaltsstoffe als funktionelle Bestandteile pflanzlicher Lebensmittel}, year = {2003}, language = {de} } @article{RohnRawelWollenbergeretal.2003, author = {Rohn, Sascha and Rawel, Harshadrai Manilal and Wollenberger, Ursula and Kroll, J{\"u}rgen}, title = {Enzyme acitivity of alpha-chymotrypsin after derivatization with phenolic compounds}, year = {2003}, language = {en} } @article{RawelKroll2003, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen}, title = {Die Bedeutung von Cassava (Manihot esculenta Crantz) als Hauptnahrungsmittel in tropischen L{\"a}ndern}, year = {2003}, language = {de} } @article{RawelRohnKroll2003, author = {Rawel, Harshadrai Manilal and Rohn, Sascha and Kroll, J{\"u}rgen}, title = {Influence of a sugar moiety (rhamnosylglycoside) at 3-O position on the reactivity of quercetin with whey proteins}, year = {2003}, language = {en} } @article{KrollRawelRohn2003, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal and Rohn, Sascha}, title = {Reactions of plant phenolics with food proteins and enzymes under special consideration of covalent bonds : a Review}, year = {2003}, language = {en} } @article{RohnRawelKroll2002, author = {Rohn, Sascha and Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen}, title = {Inhibitory effects of plant phenols on the activity of selected enzymes}, year = {2002}, abstract = {Selected enzymes (alpha-amylase, trypsin, and lysozyme) were allowed to react with some simple phenolic and related compounds (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, m-, o-, and p-dihydroxybenzenes, quinic acid, and p-benzoquinone). The derivatized enzymes obtained were characterized in terms of their activity. In vitro experiments showed that the enzymatic activity of the derivatives was adversely affected. This enzyme inhibition depended on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. The decrease in the activity was accompanied by a reduction in the amount of free amino and thiol groups, as well as tryptophan residues, which resulted from the covalent attachment of the phenolic and related compounds to these reactive nucleophilic sites in the enzymes. The enzyme inhibition correlates well with the blocking of the mentioned amino acid side chains.}, language = {en} } @article{KrollRawelCzajka2002, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal and Czajka, D{\"o}rte}, title = {Changes induced in properties of food proteins by apigenin and quercetin}, year = {2002}, abstract = {Selected food proteins (myoglobin and soy glycinin) were caused to react with flavonoids (apigenin and quercetin) to estimate the influence of the number and the position of hydroxy substituents. The protein derivatives formed have been charcterized in terms of their properties where they showed changes in the content of free amino groups, tryptophan, and thiol groups. The myoglobin derivatives have also been characterized in terms of their solubility at different pH-values to document the influence on the functional properties. The influence of myoglobin derivatives on the in vitro digestibility with trypsin was also demonstrated, with the digestion of the derivatized myoglobin being favored.}, language = {en} } @article{RohnRawelKroll2002, author = {Rohn, Sascha and Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen}, title = {Influence of plant phenols on selected enzymes}, year = {2002}, abstract = {Secondary plant metabolites are important native food components, which are becoming more and more interesting due to their physiological effects on humans. Some representatives of these compounds are very reactive and can interact with other main food components like proteins resp. enzymes. This work deals with the reactions of selected enzymes (trypsin, alpha-chymotrypsin and alpha-amylase) with simple phenolic and related substances (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, meta-, ortho- and para-dihydroxybenzene, 1,4-benzoquinone, quinic acid). The derivatives formed were characterized in terms of their activity and selected physicochemical properties. In vitro experiments showed that the proteolytic digestion of food proteins with trypsin and alpha-chymotrypsin derivatives was adversely affected. This decrease depends on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. Reactions of phenolic compounds with other enzymes (alpha-amylase and lysozyme) showed similar results with regard to physicochemical properties and their activities.}, 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} } @article{RawelCzajkaRohnetal.2002, author = {Rawel, Harshadrai Manilal and Czajka, D{\"o}rte and Rohn, Sascha and Kroll, J{\"u}rgen}, title = {Interactions of different phenolic acids and flavonoids with soy proteins}, year = {2002}, abstract = {Soy glycinin (SG) and soy trypsin inhibitor (STI) were derivatized by chlorogenic- and caffeic acid (cinnamic acids, C6 - C3 - structure), and by gallic acid representing hydroxybenzoic acids (C6 - C1 - structure). Further, the flavonoids, flavone, apigenin, kaempferol, quercetin and myricetin (C6 - C3 - C6 - structure) were also caused to react with soy proteins to estimate the influence of the number and the position of hydroxy substituents. The derivatization caused a reduction of lysine, cysteine and tryptophan residues in the soy proteins. The isoelectric points of the derivatives were shifted to lower pH values and formation of high molecular fractions was documented. The derivatives were characterized in terms of their solubility at different pH-values to document the influence on the functional properties. The structural changes induced were studied using circular dichroism (CD), differential scanning calorimetry (DSC) , intrinsic fluorescence, and binding of anilinonaphthalenesulfonic acid. The influence of derivatization on the in-vitro digestibility with trypsin, chymotrypsin, pepsin and pancreatin was also assessed. The effect on the trypsin inhibitor activity of all the resulting STI derivatives was studied, the latter being reduced.}, language = {en} } @misc{SonkajaerviRoggeDemuraetal.2004, author = {Sonkaj{\"a}rvi, Hanna and Rogge, J{\"o}rg and Demura, Shin and Fichte, Robby and Alk{\"a}mper, Urte Christine and Tischer, Anuschka and Wollschl{\"a}ger, Thomas and Prass, Reiner and Helmedach, Andreas and Kubetzky, Thomas and Mehrkens, Heidi and Kater, Thomas and Sawilla, Jan Marco and Schneider, Dorit and Uebersch{\"a}r, Ellen and Angelow, J{\"u}rgen and Muth, J{\"o}rg and Lang, Heinrich and Kroll, Stefan and Kroener, Bernhard R. and Pr{\"o}ve, Ralf and Hollberg, Cecilie}, title = {Milit{\"a}r und Gesellschaft in der Fr{\"u}hen Neuzeit}, volume = {8}, number = {1}, publisher = {Universit{\"a}tsverlag Potsdam}, address = {Potsdam}, organization = {Arbeitskreis Milit{\"a}r und Gesellschaft in der Fr{\"u}hen Neuzeit e.V. (Hrsg.)}, issn = {1617-9722}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-6765}, year = {2004}, abstract = {Aus dem Inhalt dieser Ausgabe: BEITR{\"A}GE: Hanna Sonkaj{\"a}rvi: Soldaten als Fremde in Straßburg im 18. Jahrhundert, J{\"o}rg Rogge: Das Kriegswesen im sp{\"a}ten Mittelalter und seine Erforschung: neuere englische und deutsche Arbeiten zu Krieg, Staat und Gesellschaft, PROJEKTE: Shin Demura: Allso hiebe der innere krieg schon an, der vil Erger dann der e{\"u}ssere war : die Stadt als Zufluchtsort f{\"u}r Fl{\"u}chtlinge : Erfahrungsformen des Dreißigj{\"a}hrigen Krieges in der Reichsstadt Ulm und ihrer Region, Robby Fichte: Zur Entwicklungsgeschichte des {\"o}ffentlich-rechtlichen Vertrages anhand der Begr{\"u}ndung des Milit{\"a}rdienstverh{\"a}ltnisses 1650-1914, Urte Christine Allk{\"a}mper: Die Braut des Soldaten : symbolische Kommunikation mit der Waffe von der Fr{\"u}hen Neuzeit bis zur Gegenwart, Anuschka Tischer: Offizielle Kriegsbegr{\"u}ndungen in der fr{\"u}hen Neuzeit - Funktionen, Formen, Inhalte, Thomas Wollschl{\"a}ger: Die Military Revolution und der deutsche Territorialstaat unter besonderer Ber{\"u}cksichtigung Brandenburg-Preußens und Sachsens : Determinanten der Staatskonsolidierung im europ{\"a}ischen Kontext 1670-1740, BERICHTE: Reiner Prass: Tagungsbericht Gewalt in der Fr{\"u}hen Neuzeit : 5. Tagung der Arbeitsgemeinschaft Fr{\"u}he Neuzeit vom 18. bis 20. September 2003 an der Freien Universit{\"a}t Berlin, Andreas Helmedach, Thomas Kubetzky, Heidi Mehrkens: Tilly ist nur eine Chiffre, die es aufzul{\"o}sen gilt ... - Jahrestagung des Arbeitskreises Milit{\"a}rgeschichte: Soldat und Gesellschaft : Biographien und Selbstzeugnisse in der Milit{\"a}rgeschichte 10.-11. Oktober 2003, Thomas Kater: Bericht {\"u}ber die Jahrestagung des Arbeitskreises Historische Friedensforschung : Der Friede ist keine leere Idee ... - Bilder und Vorstellungen vom Frieden im langen 19. Jahrhundert, 31.10. bis 2.11.2003, Stiftung Adam von Trott, Imshausen, Jan Marco Sawilla: Religion und Krieg - Bericht {\"u}ber die Hamburger Gespr{\"a}che zur Geschichtswissenschaft (V III.) WS 2003/ 2004, Dorit Schneider: Kriegsbegr{\"u}ndungen in der Geschichte. Strategien der Legitimierung und Legalisierung milit{\"a}rischer Gewalt - 30.-31.01.2004, Deutscher Bundestag, Berlin, REZENSIONEN: Ellen Uebersch{\"a}r: Das Strafgericht Gottes : Kriegserfahrungen und Religion im Heiligen R{\"o}mischen Reich Deutscher Nation im Zeitalter des Dreißigj{\"a}hrigen Krieges, hrsg. von Matthias Asche und Anton Schindling, M{\"u}nster 2001, J{\"u}rgen Angelow: Jutta Nowosadtko: Krieg, Gewalt und Ordnung : Einf{\"u}hrung in die Milit{\"a}rgeschichte, T{\"u}bingen 2002, J{\"o}rg Muth: John A. Lynn: Battle - A History of Combat and Culture from Ancient Greece to Modern Amerika, Boulder 2003, Heinrich Lang: Del Treppo, Mario (H g.): Condottieri e uomini d arme nell Italia del Rinascimento. Acura e con un saggio introduttivo di Mario Del Treppo, Napoli 2001, Stefan Kroll: J{\"o}rg Muth, Flucht aus dem milit{\"a}rischen Alltag : Ursachen und individuelle Auspr{\"a}gung der Desertion in der Armee Friedrichs des Großen. Mit besonderer Ber{\"u}cksichtigung der Infanterie-Regimenter der Potsdamer Garnison, Freiburg i. Br. 2003, ANK{\"U}NDIGUNGEN: Bernhard R. Kroener, Ralf Pr{\"o}ve: Tempi passati! Der Arbeitskreis Milit{\"a}r und Gesellschaft in der Fr{\"u}hen Neuzeit : ein Zwischenbericht nach einem Jahrzehnt, Mitgliederversammlung 2004, AMG-Tagung 2007, Cecilie Hollberg: Glaube \& Macht : Sachsen im Europa der Reformationszeit ; die 2. S{\"a}chsische Landesausstellung ; die Schlacht bei M{\"u}hlberg : Ausgang und Folgen}, subject = {Milit{\"a}r / Geschichte}, language = {de} } @misc{GrottPeterLinkeretal.2003, author = {Grott, Saskia and Peter, Martin G. and Linker, Torsten and Sefkow, Michael and Kroll, J{\"u}rgen and Koetz, Joachim and Laschewsky, Andr{\´e} and Lokatis, Siegfried and Rheinberg, Falko and Manig, Yvette}, title = {Portal = Chemie: Werkstoffe, Wirkstoffe, Lebensvorg{\"a}nge}, number = {01-02/2003}, organization = {Universit{\"a}t Potsdam, Referat f{\"u}r Presse- und {\"O}ffentlichkeitsarbeit}, issn = {1618-6893}, doi = {10.25932/publishup-43971}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-439713}, pages = {46}, year = {2003}, abstract = {Aus dem Inhalt: - Chemie: Werkstoffe, Wirkstoffe, Lebensvorg{\"a}nge - Institut f{\"u}r Kirchenrecht gegr{\"u}ndet - Computerlinguisten erstellen digitales W{\"o}rterbuch - Vom Spaß am Graffiti-Sprayen}, language = {de} } @article{RawelKrollRieseSchneideretal.1998, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen and Riese-Schneider, Brigitte and Haebel, Sophie}, title = {Changes in physico-chemical and enzymatic properties of benzyl isothiocyanate derivatized proteinases}, year = {1998}, language = {en} } @article{WalzelOzierenskiStarketal.1996, author = {Walzel, Erwin and Ozierenski, B{\"a}rbel and Stark, Claudia and Kroll, J{\"u}rgen}, title = {Der Einfluß von niederverestertem Pektin und Pektinabbauprodukten auf die Inkorporation von Blei bei konventionalisierten und keimfreien Ratten}, year = {1996}, language = {de} } @article{KrollJancke1994, author = {Kroll, J{\"u}rgen and Jancke, Harald J.}, title = {Reaktionen von Benzyl-ITC mit Glutathion : NMR-spektroskopische Untersuchungen}, year = {1994}, language = {de} } @book{JohnsenKrollLange1993, author = {Johnsen, Dieter and Kroll, J{\"u}rgen and Lange, Reinhard}, title = {Ern{\"a}hrung - Umwelt - Gesundheit : Teil 1}, series = {Studienmaterialien des Weiterbildenden Studiums Umweltschutz f{\"u}r Bildung und Hauswirtschaft}, journal = {Studienmaterialien des Weiterbildenden Studiums Umweltschutz f{\"u}r Bildung und Hauswirtschaft}, editor = {Berndt, Klaus-Peter and Sch{\"a}fer, Erich}, publisher = {Univ. Potsdam}, address = {Potsdam}, isbn = {3-929757-17-6}, pages = {72 S.}, year = {1993}, language = {de} } @article{KruseKroll1995, author = {Kruse, Hans-Peter and Kroll, J{\"u}rgen}, title = {Fettaustauscher : lebensmittelchemische und ern{\"a}hrungsphysiologische Aspekte}, year = {1995}, language = {de} } @article{RawelKroll1995, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen}, title = {Some aspects of reactions of benzyl isothiocyanate with bovine sarcoplasmic proteins}, year = {1995}, language = {en} } @article{WalzelKroll1995, author = {Walzel, Erwin and Kroll, J{\"u}rgen}, title = {Kritische Spurenelemente in der Ern{\"a}hrung}, year = {1995}, language = {de} } @article{KrollRawel2006, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal}, title = {Die Sojabohne : Inhalsstoffe und deren Lebensmittelchemische und ern{\"a}hrungsphysiologische Bedeutung}, issn = {0012-0431}, year = {2006}, abstract = {The soy bean contains besides comparatively large amounts of nutritionally and physiologically valuable proteins and lipids, also a series of other minor components termed as secondary plant metabolites. In this respect most of the research focus has been directed to the group of isoflavones. Epidemiological studies as well as model and animal experiments document that the consumption of soy products/-components is accompanied by many postive physiological effects, which are discussed shortly in this paper}, language = {de} } @article{StarkWalzelOzierenskietal.1995, author = {Stark, Claudia and Walzel, Erwin and Ozierenski, B{\"a}rbel and Kroll, J{\"u}rgen}, title = {Die Wirkung von Pektin bei aktueller Bleiexposition}, year = {1995}, language = {de} } @article{RawelKrollHaebeletal.1998, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen and Haebel, Sophie and Peter, Martin G.}, title = {Reactions of a glucosinolate breakdown product (benzyl-isothiocyanate) with myoglobin}, year = {1998}, language = {en} } @article{RawelKrollRieseSchneideretal.1998, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen and Riese-Schneider, Brigitte and Haebel, Sophie}, title = {Physicochemical and enzymatic properties of Benzyl-Isothiocyanate derivatized proteinases}, year = {1998}, language = {en} } @article{RawelKrollSchroeder1998, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen and Schr{\"o}der, Insa Sigrid}, title = {In vitro enzymatic digestion of benzyl- and phenylisothiocyanate derivatized food proteins}, year = {1998}, language = {en} } @article{KrollRawelKroeck1998, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal and Kr{\"o}ck, Regina}, title = {Microwave digestion of proteins}, year = {1998}, language = {en} } @article{RawelKrollSchroeder1998, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen and Schr{\"o}der, Insa Sigrid}, title = {Reactions of isothiocyanates with food proteins : influence on enzyme activity and degradation}, year = {1998}, language = {en} } @article{KrollRawel1996, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal}, title = {Chemical reactions of benzyl isothiocyanate with myoglobin}, year = {1996}, language = {en} } @article{KrollHelle1994, author = {Kroll, J{\"u}rgen and Helle, N.}, title = {Mechanochemischer Abbau von Proteinen : ESR - spektroskopische Untersuchungen}, year = {1994}, language = {de} } @article{KrollRawel2001, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal}, title = {Reactions of plant phenols with myoglobin : influence of chemical structure of the phenolic compounds}, year = {2001}, language = {en} } @article{RawelKrollHohl2001, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen and Hohl, U. C.}, title = {Model studies on reactions of plant phenols with whey proteins}, year = {2001}, language = {en} } @article{KrollRawelRohnetal.2001, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal and Rohn, Sascha and Czajka, D{\"o}rte}, title = {Interactions of glycinin with plant phenols : influence on chemical properties and proteolytic degradation of the proteins}, year = {2001}, abstract = {Soya glycinin was derivatized with different phenolic substances (caffeic-, chlorogenic-, gallic acid and quercetin). The protein derivatives formed have been characterized in terms of their properties where they showed changes in the content of free epsilon-amino groups, tryptophan and thiol groups. The derivatives have also been characterized in terms of their solubility at different pH-values to document the influence on the functional properties. Another objective of this paper was to demonstrate the influence on the digestibility of the proteins with one of the main enzymes of the gastro-intestinal tract (pancreatin) on the basis of in vitro experiments after derivatization with phenolic substances. The enzymatic digestion of the derivatized proteins was promoted.}, language = {en} } @article{RohnRawelPietruschinskietal.2001, author = {Rohn, Sascha and Rawel, Harshadrai Manilal and Pietruschinski, Nadine and Kroll, J{\"u}rgen}, title = {In vitro inhibition of alpha -chymotryptic activity by phenolic compounds}, year = {2001}, abstract = {alpha-Chymotrypsin was modified by covalent attachment of selected phenolic and related compounds (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, quinic acid, m-/o-/p-dihydroxybenzene and p-benzoquinone) at pH 9. The derivatives formed were characterised in terms of their activity and selected physicochemical properties. In vitro experiments showed that the proteolytic digestion of food proteins with alpha-chymotrypsin derivatives was adversely affected. This decrease depended on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. The derivatisation was accompanied by a reduction in the amount of free lysine and tryptophan residues. Moreover, the solubility of the derivatives decreased over a broad pH range, with a parallel increase in the hydrophobicity. The isoelectric point was shifted to a lower pH value, and formation of high-molecular-weight fractions was documented by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE).}, language = {en} } @article{RawelKrollRiese2000, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen and Riese, B.}, title = {Reaction of chlorogenic acid with lysozyme : physicochemical characterization and proteolytic digestion of the derivatives}, year = {2000}, language = {en} } @article{KrollRawel2000, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal}, title = {Reactions of plant phenols with myoglobin : influence of chemical structure of the phenolic compounds}, year = {2000}, language = {en} } @article{KrollRawelSeidelmann2000, author = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal and Seidelmann, N.}, title = {Physicochemical properties and susceptibility to proteolytic digestionof myoglobin-phenol derivatives}, year = {2000}, language = {en} } @article{RawelKrollRohn2000, author = {Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen and Rohn, Sascha}, title = {Reactions of phenol substances with lysozyme - physicochemical characterisation and proteolytic digestion of the derivatives}, year = {2000}, language = {en} } @article{RawelRohnKroll2000, author = {Rawel, Harshadrai Manilal and Rohn, Sascha and Kroll, J{\"u}rgen}, title = {Reactions of selected secondary plant metabolites (glucosinolates and phenols) with food proteins and enzymes - Influence on physicochemical properties, enzyme activity and proteolytic dagradation}, year = {2000}, language = {en} }