@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{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{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{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{KrollRawel1996,
  author    = {Kroll, J{\"u}rgen and Rawel, Harshadrai Manilal},
  title     = {Chemical reactions of benzyl isothiocyanate with myoglobin},
  year      = {1996},
  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{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     = {In vitro enzymatic digestion of benzyl- and phenylisothiocyanate derivatized food proteins},
  year      = {1998},
  language  = {en}
}