Influencing emulsifying properties of egg yolk by enzymatic modification with phospholipase D. Part 2: Structural changes of egg yolk due to incubation

This work characterizes the emulsifying properties of systems containing egg yolk (0.1; 1.0 and 2.5 % w/v) and polysaccharides (xanthan gum, carrageen, pectin and carboxymethylcellulose) and three different vegetable oils (sunflower, canola, and palm oils). Emulsifying activity and emulsion stability were measured of each combination and it was found the effect of the oil on emulsion stability correlated to the amount of monounsaturated fatty acid. Additionally, increased egg yolk concentration increased emulsifying activity by reducing coalescence of oil droplets. Lastly, 2.5% egg yolk and 0.2% polysaccharide generated emulsions with high emulsifying activity, excellent stability, and droplet size of 4.32 µm.

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Emulsifying Properties of Cholesterol-Reduced Egg Yolk Low-Density Lipoprotein

ACS Symposium Series - Functional Properties of Proteins and Lipids ◽

10.1021/bk-1998-0708.ch013 ◽

1998 ◽

pp. 205-217

Author(s):

Yoshinori Mine ◽

Marie Bergougnoux

Keyword(s):

Low Density Lipoprotein ◽

Density Lipoprotein ◽

Egg Yolk ◽

Low Density ◽

Emulsifying Properties

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Effect of enzymatic hydrolysis on heat stability and emulsifying properties of egg yolk

Food Hydrocolloids ◽

10.1016/j.foodhyd.2019.105224 ◽

2019 ◽

Vol 97 ◽

pp. 105224 ◽

Cited By ~ 6

Author(s):

Yang Gao ◽

Junhua Li ◽

Cuihua Chang ◽

Chenying Wang ◽

Yanjun Yang ◽

...

Keyword(s):

Enzymatic Hydrolysis ◽

Egg Yolk ◽

Heat Stability ◽

Emulsifying Properties

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FRACTIONATION AND DISSOCIATION OF THE AVIAN LIPOVITELLINS AND THEIR INTERACTION WITH PHOSVITIN

Canadian Journal of Biochemistry ◽

10.1139/o64-047 ◽

1964 ◽

Vol 42 (3) ◽

pp. 395-406 ◽

Cited By ~ 15

Author(s):

M. W. Radomski ◽

W. H. Cook

Keyword(s):

Ionic Strength ◽

Phosphate Buffer ◽

Structural Changes ◽

Phosphorus Content ◽

Egg Yolk ◽

Gradient Elution ◽

Progressive Change ◽

Hen’S Egg ◽

Dowex 1 ◽

Elution Chromatography

Phosvitin and lipovitellin, the granule proteins of hen's egg yolk, were clearly separated by gradient elution on Dowex-1 columns. No phosvitin could be detected in the lipovitellin fraction but the first eluates of the phosvitin fraction contained lipovitellin of high protein phosphorus content. These initial eluates contained only two components sedimenting at rates slightly higher than dimer and monomer lipovitellin. As the lipovitellin monomer does not ordinarily occur in neutral solvents, the slower sedimenting material is either a new component or the monomer stabilized through interaction with phosvitin.Gradient elution chromatography of the total lipovitellins on hydroxyapatite showed that β-lipovitellin was completely eluted by 0.6 M phosphate buffer at pH 6.8 and appeared to be homogeneous. However, α-lipovitellin was heterogeneous: it was eluted over a concentration range of 0.7 to 1.4 M and the protein phosphorus content and dissociative behavior of successive fractions showed a progressive change with increasing ionic strength. Superimposed on this general heterogeneity of α-lipovitellin, there was consistent evidence of two poorly defined components, and three when the α-fraction was rechromatographed. Following dissociation and reassociation, there was no evidence of hybridization between monomers of α- and β-lipovitellin. Changes in the chromatographic patterns of α-lipovitellin following dissociation may indicate hybridization of different α-monomers, but these could also arise from structural changes in the monomers.

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