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

Kód výsledku v 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>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

GM - Potravinářství

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2009

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Czech Journal of Food Sciences

ISSN

1212-1800

e-ISSN

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Svazek periodika

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Číslo periodika v rámci svazku

27

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

5

Strana od-do

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Kód UT WoS článku

000269005600002

EID výsledku v databázi Scopus

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