@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{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{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{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}
}