@article{ReinkensmeierSteinbrennerHomannetal.2016,
  author    = {Reinkensmeier, Annika and Steinbrenner, Katrin and Homann, Thomas and Bussler, Sara and Rohn, Sascha and Rawel, Harshadrai Manilal},
  title     = {Monitoring the apple polyphenol oxidase-modulated adduct formation of phenolic and amino compounds},
  series = {Food chemistry},
  volume    = {194},
  journal   = {Food chemistry},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0308-8146},
  doi       = {10.1016/j.foodchem.2015.07.145},
  pages     = {76 -- 85},
  year      = {2016},
  abstract  = {Minimally processed fruit products such as smoothies are increasingly coming into demand. However, they are often combined with dairy ingredients. In this combination, phenolic compounds, polyphenoloxidases, and amino compounds could interact. In this work, a model approach is presented where apple serves as a source for a high polyphenoloxidase activity for modulating the reactions. The polyphenoloxidase activity ranged from 128 to 333 nakt/mL in different apple varieties. From these, 'Braeburn' was found to provide the highest enzymatic activity. The formation and stability of resulting chromogenic conjugates was investigated. The results show that such adducts are not stable and possible degradation mechanisms leading to follow-up products formed are proposed. Finally, apple extracts were used to modify proteins and their functional properties characterized. There were retaining antioxidant properties inherent to phenolic compounds after adduct formation. Consequently, such interactions may also be utilized to improve the textural quality of food products.},
  language  = {en}
}
@article{ReinkensmeierBasslerSchlueteretal.2015,
  author    = {Reinkensmeier, Annika and Bassler, Sara and Schlueter, Oliver and Rohn, Sascha and Rawel, Harshadrai Manilal},
  title     = {Characterization of individual proteins in pea protein isolates and air classified samples},
  series = {Food research international},
  volume    = {76},
  journal   = {Food research international},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0963-9969},
  doi       = {10.1016/j.foodres.2015.05.009},
  pages     = {160 -- 167},
  year      = {2015},
  abstract  = {Generally, pea proteins are extracted at comparatively acidic or basic pH values to provide a basis for protein isolate production. Such processing steps result in partial denaturation of the proteins rendering them in most cases insoluble at food processing pH conditions and limiting their application in food products. Here, the comparison of the solubility properties of pea proteins in protein enriched fractions deriving from air classification is reported. Protein content, solubility, and physicochemical parameters of different fractions of the pea (Pisum sativum) variety 'Salamanca' were investigated as a function of pH using SDS-PAGE and surface hydrophobicity. Whole pea flour (20\% protein), air classified, protein-enriched pea flour (48\% protein), pea flour made from hulls (2.8\% protein), and pea protein isolate (81\% protein) served as test materials. Fractionation and pH value affected the composition and surface hydrophobicity of the proteins as well as the content of trypsin inhibitors. All samples showed a high buffering capacity in the range of pH 4 to 10. The direct comparison documents the comparatively better protein quality of the air classified, protein enriched pea fraction. The solubility of the pea protein isolate can be improved by using selected additives, giving new possibilities for plant protein application. Relevant technofunctional properties were determined and compared with two commercially available pea-based products (whole pea flour and an isolate). Water binding capacity was highest for the commercially available pea flour followed by the pea hull flour. Fat binding capacity remained more or less unchanged. (C) 2015 Elsevier Ltd. All rights reserved.},
  language  = {en}
}