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- W1971812169 abstract "This study characterized the impact of technological treatments on the protein secondary structure of a newly developed egg yolk livetin formulation and its components α-livetin, which is identical with chicken serum albumin, and γ-livetin, the bioactive antibody immunoglobulin Y. Fourier transform infrared (FTIR) spectroscopy at 25 °C revealed that the largest proportion of conformal elements comprised intramolecular (native) β-sheets (60-80%) in γ-livetin, and α-helices/random coils (60.59%) in α-livetin. In reconstituted freeze-dried livetins, the main protein conformations were also intramolecular (native) β-sheets (55.08%) and α-helices/random coils (30.51%), but upon heating from 25 to 95 °C, the former decreased sigmoidally at the onset-of-denaturation temperature (TOD (FTIR)) of 69.5 °C, concomitant with a sigmoidal increase in intermolecular (denatured) β-sheets at a TOD (FTIR) of 72.4 °C and a sigmoidal decrease in IgY activity at TOD (ELISA) of 67.5 °C. Reconstituted spray-dried livetins showed less native β-sheets and significantly lower TOD (FTIR) values than freeze-dried livetins." @default.
- W1971812169 created "2016-06-24" @default.
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- W1971812169 date "2015-04-01" @default.
- W1971812169 modified "2023-10-10" @default.
- W1971812169 title "Determination of heat-induced changes in the protein secondary structure of reconstituted livetins (water-soluble proteins from hen’s egg yolk) by FTIR" @default.
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- W1971812169 doi "https://doi.org/10.1016/j.foodchem.2014.09.128" @default.
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