TY - JOUR A1 - Rohn, Sascha A1 - Rawel, Harshadrai Manilal A1 - Kroll, Jürgen T1 - Antioxidant activity of protein-bound quercetin N2 - 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. Y1 - 2004 UR - http://pubs.acs.org/cgi-bin/article.cgi/jafcau/2004/52/i15/html/jf0496797.html ER - TY - JOUR A1 - Rawel, Harshadrai Manilal A1 - Ranters, Holger A1 - Rohn, Sascha A1 - Kroll, Jürgen T1 - Assessment of the reactivity of selected isoflavones against proteins in comparison to quercetin N2 - 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. Y1 - 2004 UR - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15291506 ER - TY - JOUR A1 - Hernandez-Triana, Manuel A1 - Kroll, Jürgen A1 - Proll, Jürgen A1 - Noack, Jutta A1 - Petzke, Klaus-Jürgen T1 - Benzyl-isothiocyanate (BITC) decreases quality of egg white proteins in rats Y1 - 1996 ER - TY - JOUR A1 - Rawel, Harshadrai Manilal A1 - Meidtner, Karina A1 - Kroll, Jürgen T1 - Binding of selected phenolic compounds to proteins N2 - 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 Y1 - 2005 SN - 0021-8561 ER - TY - JOUR A1 - Rawel, Harshadrai Manilal A1 - Kroll, Jürgen A1 - Riese-Schneider, Brigitte A1 - Haebel, Sophie T1 - Changes in physico-chemical and enzymatic properties of benzyl isothiocyanate derivatized proteinases Y1 - 1998 ER - TY - JOUR A1 - Kroll, Jürgen A1 - Rawel, Harshadrai Manilal A1 - Czajka, Dörte T1 - Changes induced in properties of food proteins by apigenin and quercetin N2 - 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. Y1 - 2002 ER - TY - JOUR A1 - Rawel, Harshadrai Manilal A1 - Rohn, Sascha A1 - Kroll, Jürgen T1 - Characterisation of 11S protein fractions and phenolic compounds from green coffee beans under special consideration of their interactions - A review N2 - 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 Y1 - 2005 SN - 0012-0413 ER - TY - JOUR A1 - Kroll, Jürgen A1 - Noack, Jutta A1 - Rawel, Harshadrai Manilal A1 - Kröck, Regina A1 - Proll, Jürgen T1 - Chemical reactions of benzyl isothio cyanate with egg-white protein fractions Y1 - 1994 ER - TY - JOUR A1 - Kroll, Jürgen A1 - Rawel, Harshadrai Manilal T1 - Chemical reactions of benzyl isothiocyanate with myoglobin Y1 - 1996 ER - TY - JOUR A1 - Petzke, Klaus-Jürgen A1 - Schuppe, S. A1 - Rohn, Sascha A1 - Rawel, Harshadrai Manilal A1 - Kroll, Jürgen T1 - Chlorogenic acid moderately decreases the quality of whey proteins in rats N2 - 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 Y1 - 2005 SN - 0021-8561 ER - TY - JOUR A1 - Walzel, Erwin A1 - Ozierenski, Bärbel A1 - Stark, Claudia A1 - Kroll, Jürgen T1 - Der Einfluß von niederverestertem Pektin und Pektinabbauprodukten auf die Inkorporation von Blei bei konventionalisierten und keimfreien Ratten Y1 - 1996 ER - TY - JOUR A1 - Rawel, Harshadrai Manilal A1 - Frey, Simone K. A1 - Meidtner, Karina A1 - Kroll, Jürgen A1 - Schweigert, Florian J. T1 - Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence JF - Molecular nutrition & food research : bioactivity, chemistry, immunology, microbiology, safety, technology N2 - 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. KW - amylase activity KW - green tea phenols KW - protein-phenol binding KW - saliva proteins KW - tryptophan quenching Y1 - 2006 U6 - https://doi.org/10.1002/mnfr.200600013 SN - 1613-4125 VL - 50 IS - 8 SP - 705 EP - 713 PB - Wiley CY - Weinheim ER - TY - JOUR A1 - Rawel, Harshadrai Manilal A1 - Kroll, Jürgen T1 - Die Bedeutung von Cassava (Manihot esculenta Crantz) als Hauptnahrungsmittel in tropischen Ländern Y1 - 2003 ER - TY - JOUR A1 - Kroll, Jürgen A1 - Rawel, Harshadrai Manilal T1 - Die Sojabohne : Inhalsstoffe und deren Lebensmittelchemische und ernährungsphysiologische Bedeutung N2 - 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 Y1 - 2006 SN - 0012-0431 ER - TY - JOUR A1 - Stark, Claudia A1 - Walzel, Erwin A1 - Ozierenski, Bärbel A1 - Kroll, Jürgen T1 - Die Wirkung von Pektin bei aktueller Bleiexposition Y1 - 1995 ER - TY - JOUR A1 - Kroll, Jürgen A1 - Rohn, Sascha A1 - Rawel, Harshadrai Manilal T1 - Einsatz von MALDI- und SELDI-Massenspectrometrie zur Charakterisierung ausgewählten Nahrungsproteine und Proteinmodifikationen N2 - 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. Y1 - 2004 SN - 0250-1554 ER - TY - JOUR A1 - Rohn, Sascha A1 - Rawel, Harshadrai Manilal A1 - Wollenberger, Ursula A1 - Kroll, Jürgen T1 - Enzyme acitivity of alpha-chymotrypsin after derivatization with phenolic compounds Y1 - 2003 ER - TY - BOOK A1 - Johnsen, Dieter A1 - Kroll, Jürgen A1 - Lange, Reinhard ED - Berndt, Klaus-Peter ED - Schäfer, Erich T1 - Ernährung - Umwelt - Gesundheit : Teil 1 T3 - Studienmaterialien des Weiterbildenden Studiums Umweltschutz für Bildung und Hauswirtschaft Y1 - 1993 SN - 3-929757-17-6 PB - Univ. Potsdam CY - Potsdam ER - TY - JOUR A1 - Kruse, Hans-Peter A1 - Kroll, Jürgen T1 - Fettaustauscher : lebensmittelchemische und ernährungsphysiologische Aspekte Y1 - 1995 ER - TY - JOUR A1 - Rawel, Harshadrai Manilal A1 - Kroll, Jürgen A1 - Schröder, Insa Sigrid T1 - In vitro enzymatic digestion of benzyl- and phenylisothiocyanate derivatized food proteins Y1 - 1998 ER -