The Chemistry of Eggs and Egg Products

Powrie, W.; Nakai, S.

doi:10.1007/978-1-349-09142-3_6

Cited by 99 publications

(99 citation statements)

References 209 publications

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“…19,20 Three proton pools or peaks correlating to these three major components were expected in the CPMG spectra of yolk. Because large biomolecules possess faster spin-spin relaxation times than smaller molecules such as water, 21 the peak with the smallest T2, indicating the fastest relaxing and least mobile components, could be attributed to the yolk proteins.…”

Section: Resultsmentioning

confidence: 98%

Determination of the Gelation Mechanism of Freeze–Thawed Hen Egg Yolk

Acevedo

Horner

et al. 2015

J. Agric. Food Chem.

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A study of yolks stored up to 168 d at −20 °C was conducted to determine the gelation behavior and mechanism of freeze–thawed yolk. Methods used were rheology, native and sodium dodecyl sulfate polyacrylamide gel electrophoresis (native- and SDS-PAGE), differential scanning calorimetry (DSC), transmission electron microscopy (TEM), particle size analysis, and proton nuclear magnetic resonance (1H NMR) spectroscopy for matrix mobility. Results indicate that both constituents of plasma and granules contributed to gelation of yolk under freezing. PAGE analyses suggest that granular proteins participated in aggregation during freeze–thaw. Increasing gel strength and particle size and decreasing water and lipid–water mobility indicate that lipoproteins or apolipoproteins aggregated. At storage times ≥84 d, increased protein and lipid mobility, the detection of smaller particles, and secondarily increased gel strength suggest the liberation of protein or lipoprotein components from previously formed aggregates and further aggregation of these constituents. Disruption of the gelled yolk matrix observed with TEM supported that ice crystal formation was required for gelation to occur. A two-stage dynamic gelation model is thus proposed.

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Section: Resultsmentioning

confidence: 98%

Determination of the Gelation Mechanism of Freeze–Thawed Hen Egg Yolk

Acevedo

Horner

et al. 2015

J. Agric. Food Chem.

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“…The molecular weights of these proteins range from 12,000 to 8,000,000 Daltons consisting of ovomucin fibres conalbumin, ovomucoid, lysozyme, globulins, and ovomucin in an aqueous solution of numerous globular proteins (Powrie and Nakai, 1986). Protein film materials are characterized by high moisture permeability, low oxygen and lipid permeability at lower relative humidity.…”

Section: Introductionmentioning

confidence: 99%

Effect of different concentrations of olive oil and oleic acid on the mechanical properties of albumen (egg white) edible films

Taqi¹,

Askar²,

Nagy³

et al. 2011

Afr. J. Biotechnol.

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The main objective of this study was to investigate the effect of olive oil and oleic acid addition to albumin (egg white) through emulsification to produce films on mechanical properties. Plasticizer was necessary to maintain film and coating integrity and to avoid pores cracks. Edible composite films were prepared from albumin and lipid material at (1 and 1.5%), respectively. The effect of unsaturated oleic acid with glycerol and monounsaturated olive oil on tensile strength, elongation at break, water vapor permeability (WVP), opacity (OP), solubility, colour and atomic force microscopy (AFM) was investigated. In general, the incorporation of lipid materials resulted in the increase (P < 0.05) of tensile strength and elongation at break, and the reduction of WVP with some exceptions. Overall, the effect of monounsaturated was greater than that of unsaturated. The surface microstructure of the films was analyzed using atomic force microscopy (AFM).

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“…The commercial preparations are often sold as "ovalbumin" but it is a mixture of egg white proteins (EFSA 2011b): the major one is albumin (Ovalbumin) which represents 54% of the egg white protein. Other major proteins are Conalbumin (Ovotransferrin) (12%), Ovomucoid (11%), Ovomucin (3.5%), and Lysozyme (3.4%) (Powrie et al 1985;Walsh et al 1988).…”

Section: Proteins Used In Winemaking and Possible Drawbacks Related Tmentioning

confidence: 99%

Hidden exogenous proteins in wine: problems, methods of detection and related legislation - a review

Rizzi¹,

Mainente²,

Pasini³

et al. 2016

Czech J. Food Sci.

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Rizzi C., Mainente F., Pasini G., Simonato B. (2016): Hidden exogenous proteins in wine: problems, methods of detection and related legislation -a review. Czech J. Food Sci., 34: 93-104.Fining agents are commonly used in the winemaking process to clarify and stabilise wines. They have different origins (animal, vegetal or mineral) and are added to wines in order to remove specifically undesirable compounds that are discarded. Fining agents should not be present in the final product but their possible persistence, as well as other exogenous residual proteins such as the enzymes utilised in winemaking, cannot be excluded for sure. The principal concern about the presence of exogenous residual proteins is the health of allergic subjects. Nevertheless, the respect of religious creed or other practice of living of the consumer must be considered as well. In the present review we itemise the proteins used in winemaking and possible drawbacks of their permanence in the final products and the related risks, depict the status of the art of the studies performed about the detection of exogenous proteins, and describe the wine labelling laws adopted in different countries to avoid the drawbacks associated with these hidden substances.

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The Chemistry of Eggs and Egg Products

Cited by 99 publications

References 209 publications

Determination of the Gelation Mechanism of Freeze–Thawed Hen Egg Yolk

Determination of the Gelation Mechanism of Freeze–Thawed Hen Egg Yolk

Effect of different concentrations of olive oil and oleic acid on the mechanical properties of albumen (egg white) edible films

Hidden exogenous proteins in wine: problems, methods of detection and related legislation - a review

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