The characterization of whey proteins-pectin interaction in relation to emulsification properties of whey proteins.

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F09%3A00022447" target="_blank" >RIV/60461373:22330/09:00022447 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
The characterization of whey proteins-pectin interaction in relation to emulsification properties of whey proteins.
Original language description
The aim of this work was to characterise influence of whey proteins?pectin interaction on emulsification properties of whey. As the first, structural characteristics of pectin-protein complexes were evaluated for pure ?-actoglobulin by both dynamic lightscattering method for measuring of the particle size distributions and Doppler laser electrophoresis for measuring the potential (surface electrical potential) of particles. In mixed pectin-?-actoglobulin systems, it was observed that the addition of pectin prevent from the protein-protein interaction, which caused production of huge protein aggregates (2000-2500 nm) at pH values near ?-lactoglobulin isoelectric point and at temperatures near its denaturation temperature. However, these protei?pectin complexes had large hydrodynamic diameters (monomodal size distribution at 350 and 1000 nm for high esterified and low esterified amidated pectin, resp.), which can slow down their diffusion to the oil-water interface in emulsions. The pot
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
GM - Food industry
OECD FORD branch
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Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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