@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{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{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}
}