@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{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{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{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{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{KrollJancke1994,
  author    = {Kroll, J{\"u}rgen and Jancke, Harald J.},
  title     = {Reaktionen von Benzyl-ITC mit Glutathion : NMR-spektroskopische Untersuchungen},
  year      = {1994},
  language  = {de}
}
@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{KrollHelle1994,
  author    = {Kroll, J{\"u}rgen and Helle, N.},
  title     = {Mechanochemischer Abbau von Proteinen : ESR - spektroskopische Untersuchungen},
  year      = {1994},
  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{WalzelKroll1995,
  author    = {Walzel, Erwin and Kroll, J{\"u}rgen},
  title     = {Kritische Spurenelemente in der Ern{\"a}hrung},
  year      = {1995},
  language  = {de}
}