The chemical composition of eggs

Parkinson, T. L.

doi:10.1002/jsfa.2740170301

Cited by 103 publications

(46 citation statements)

References 92 publications

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“…Egg whites consisted of 85 g/100 g water, 10 g/100 g protein, and 5 g/100 g other components such as lipid, carbohydrate, and ash (Stadelman & Cotterill, 1977). The protein compositions in egg whites are 54 g/100 g ovalbumin, 13 g/100 g conalbumin, 11 g/100 g ovomucoid, and 22 g/100 g others (Parkinson, 1966).…”

Section: Methodsmentioning

confidence: 99%

Dielectric properties of egg whites and whole eggs as influenced by thermal treatments

Wang

Tang

Wang

et al. 2009

LWT - Food Science and Technology

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Section: Methodsmentioning

confidence: 99%

Dielectric properties of egg whites and whole eggs as influenced by thermal treatments

Wang

Tang

Wang

et al. 2009

LWT - Food Science and Technology

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“…Previously, it has been suggested that LOX1 had a greater affinity for charged substrates and a lower affinity for neutral ones, regardless of the pH of the solution (24), and interacted with monomeric substrate rather than with fatty acid inserted into detergent micelles. However, the results obtained in this study clearly show that LOX1 had a greater affinity for the fatty acid inserted into the PDM-micelles than for the monomeric substrate.…”

Section: Effect Of Ph and Ionic Strength On The Ph Activity Profilementioning

confidence: 99%

Change in the Positional Specificity of Lipoxygenase 1 Due to Insertion of Fatty Acids into Phosphatidylcholine Deoxycholate Mixed Micelles

1999

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Linoleic and arachidonic acids were inserted into phosphatidylcholine deoxycholate mixed micelles (PDM-micelles) with their tail groups buried inside and carboxylic groups exposed outside. The fatty acid hydrophobic tail had a high affinity for the hydrophobic region of phosphatidylcholine micelles. The fatty acids inserted into phosphatidylcholine micelles were better substrates for soybean lipoxygenase 1 (LOX1) with two distinct pH optima at 7.0 and 10.0. With Tween 20-solubilized linoleic acid, the enzyme had a pH optimum at 9.0, exclusively forming 13-hydroperoxides. However, with linoleic and arachidonic acids inserted into PDM-micelles, LOX1 synthesized exclusively 9- and 5-hydroperoxides, respectively. The enzyme brought about the transformation of the substrate either at pH 7.4 or at 10.0, less efficiently at pH 10.0. However, the regioselectivity of the enzyme was not altered by increasing the pH from 7.4 to 10.0. Thus, LOX1 could utilize fatty acids bound to membranes as physiological substrates. The enzyme utilized the carboxylic group of linoleic and arachidonic acids inserted into the PDM-micelles as a recognition site to convert the compounds into 9- and 5-hydroperoxides, respectively. This was confirmed by activity measurements using methyl linoleate as the substrate. Circular dichroism measurement of LOX1 with PDM-micelles suggested that while there was a small change in the tertiary structure of LOX1, the secondary structure was unaffected. Soybean LOX1, which is arachidonate 15-LOX, acted as "5-LOX", thus making it possible to change the regiospecificity of the LOX1-catalyzed reaction by altering the physical state of the substrate.

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“…Yolk lipid thus exists associating with protein as lipoprotein. 16) IgY is one of the live tins (y-livetin). Therefore, removal of the lipoprotein (or lipid) is an important step for the purification ofIgY.…”

Section: Discussionmentioning

confidence: 99%

A Novel Isolation Method for Hen Egg Yolk Antibody, “IgY”

Hatta¹,

Kim²,

Yamamoto

1990

Agricultural and Biological Chemistry

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The chemical composition of eggs

Abstract: Published work on the chemical composition of eggs, with particular reference to the protein and lipid constituents, is reviewed and summarised.

Cited by 103 publications

References 92 publications

Dielectric properties of egg whites and whole eggs as influenced by thermal treatments

Dielectric properties of egg whites and whole eggs as influenced by thermal treatments

Change in the Positional Specificity of Lipoxygenase 1 Due to Insertion of Fatty Acids into Phosphatidylcholine Deoxycholate Mixed Micelles

A Novel Isolation Method for Hen Egg Yolk Antibody, “IgY”

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