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  • 1
    Electronic Resource
    Electronic Resource
    Metallic Cations Affect Functional Performance of Spray-Dried Heat-Treated Egg White (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 57 (1992), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The functional performance of four metallic cations (Cu++, Al+++, Fe+++, Zn++) in spray-dried, heat-treated egg white were evaluated. Cu++ excelled in all functional categories involving foams and angel food cakes. Zn++ was least effective. These data suggest that Cu++ would be a suitable additive to spray-dried egg white systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1992.tb06846.x
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  • 2
    Electronic Resource
    Electronic Resource
    Texture and Microstructure of Cooked Whole Egg Yolks and Heat-Formed Gels of Stirred Egg Yolk (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Hardness, cohesiveness, and springiness of heated intact egg yolks were determined by an Instron compression test. Hardness increased as temperature was increased from 75° to 90°C and as time of heating was increased from 10 to 30 min. Cohesiveness and springiness increased as temperature was increased from 75° to 80°C and as time was increased from 10 to 30 min. Egg yolks from cooked shell eggs were lower in all textural parameters than gels formed from stirred egg yolk. Low scores for cohesiveness and springiness were indicative of the crumbliness of yolk from cooked shell eggs; crumbliness was attributed to structural characteristics. The microstructure consisted of adjoining polyhedral grains, which showed no evidence of crosslinking. Grains appeared to be equivalent to yolk spheres, ranging in size from 40 to 100 μm. The structure of a stirred yolk gel consisted of a highly crosslinked protein matrix containing spheres (5–35 μm) and granules (l–2 μm).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1987.tb13973.x
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  • 3
    Electronic Resource
    Electronic Resource
    HYDROGEN PEROXIDE OXIDATION AND COAGULATION OF EGG WHITE (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 37 (1972), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1972.tb02692.x
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  • 4
    Electronic Resource
    Electronic Resource
    Texture and Microstructure of Heat-Formed Egg White Gels (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 51 (1986), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Egg white gels were formed by heating liquid egg white at various pH, protein, and NaCl levels at different temperatures and times of heating. Hardness, cohesiveness, and springiness of gels were measured. Serum was expressed from gels and evaluated by polyacrylamide gel electrophoresis. Selected samples were prepared for scanning electron microscopy. Gel hardness rose with increasing temperature, time, pH, and protein level, and decreased with added salt. Cohesiveness and springiness increased with time and temperature of heating. Expressed serum decreased as pH, time, temperature, and protein level were increased. Gels at pH 5 and 6 had a coarse, aggregated structure. At pH 9 protein strands and globules were arranged in a uniform matrix. Salt prompted aggregation of gels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1986.tb11123.x
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  • 5
    Electronic Resource
    Electronic Resource
    Ion-Exchange Chromatographic Determination of Lysozyme in Egg White (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 46 (1981), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Pure lysozyme solutions were chromatographed on diethylaminoethyl (DEAE) cellulose then monitored spectrophotometrically and by biological activity measurement. Although some biological activity was lost during chromatography, standard curves relating enzyme content to chromatographic peak area corrected for this loss. The experimental system produced egg white lysozyme concentrations which were comparable to literature values. The method of determination could be used in the comparison of total enzyme concentration to active enzyme in experimental egg products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1981.tb04497.x
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  • 6
    Electronic Resource
    Electronic Resource
    Electrophoretic and Chromatographic Changes in Egg Yolk Proteins Due to Heat (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 46 (1981), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Polyacrylamide gel electrophoresis and diethylaminoethyl-cellulose ion-exchange chromatography were used to observe changes in egg yolk products which were heat treated at 3°C intervals from 54 to 84°C for 3.5 min. The USDA pasteurization temperatures of 61.0, 63.3°C for plain, 10% sugared, and 10% salted egg yolk, respectively, had little effect on their electrophoretograms. Only the γ-livetins in plain yolk were slightly affected. Higher temperatures progressively altered these proteins until they disappeared from the electrophoretograms from plain yolk ca 73°, sugared yolk ca 76°, and salted yolk ca 79°C. The lipovitellin fraction and phosvitins were similarly affected by increasing temperatures. Sugar and salt at 10% levels had a protective effect against heat, allowing respectively ca 3° and 6°C higher temperatures before heat damage occurred. The chromatograms from plain and sugared yolk were little affected by pasteurization. However, major changes were noted between unheated and pasteurized (63.3°C) salted yolk. Patterns for salted yolk, pasteurized at 63.3 and 68.0°C were similar, which further indicated that this product can be pasteurized at 68.0°C without significant damage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1981.tb02971.x
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  • 7
    Electronic Resource
    Electronic Resource
    ION-EXCHANGE CHROMATOGRAPHY AND ELECTROPHORESIS OF EGG YOLK PROTEINS (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Pure egg yolk was fractionated using DEAE ion-exchange cellulose. Eluted components were simultaneously, detected by fluorescence and ultra-violet absorption. Selected chromatographic fractions were subjected to disc gel electrophoresis and assayed for total lipids, amino acids and phosphorus. Native egg yolk was separated into 18 peaks chromatographically and 23 bands electrophoretically. Multi-component chromatographic peaks were demonstrated by electrophoresis. Chromatographic peaks and corresponding electrophoretic bands, were identified by literature reference for lipovitellin, livetins, phosvitin and a low density fraction. A direct relationship existed between chromatographic position and electrophoretic mohility. Lipid and phosphorus concentrations were high in the same fractions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1979.tb08469.x
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  • 8
    Electronic Resource
    Electronic Resource
    CHROMATOGRAPHY AND ELECTROPHORESIS OF NATIVE AND SPRAY-DRIED EGG WHITE (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Effects of the spray-drying process on egg white proteins were studied by diethylaminoethyl cellulose ion-exchange chromatography and polyacrylamide gel electrophoresis. Major chromatographic peaks of native egg white were characterized by electrophoresis. Chromatograms and electrophoretographs of native egg white were compared to those of egg white which was adjusted to various pH levels, then spray-dried. Changes in spray-dried egg white protein patterns were minor, even at pH levels where conalbumin is heat sensitive. Egg white globulin proteins appear most sensitive to the spray-drying process. Large scale denaturation of egg white protein does not occur during spray-drying, but may initiate changes in the protein which affect the functional properties of rehydrated products. Globulin proteins require further characterization in order to properly describe their electrophoretic and chromatographic behavior.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1979.tb06435.x
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  • 9
    Electronic Resource
    Electronic Resource
    Texture Profile Analysis, Expressed Serum, and Microstructure of Heat-Formed Egg Yolk Gels (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Egg yolk gels were formed by heating previously stirred egg yolk, having various pHs, protein concentrations, and NaCl levels, at various times and temperatures. Texture profiles were obtained by an Instron double-compression test, and serum was expressed from frozen-thawed gels. Microstructures of selected gels were observed by scanning electron microscopy. Gel hardness generally increased with increasing pH, protein or salt concentration, temperature, and length of heating time. The amount of serum expressed from gels decreased as gel hardness increased. Cohesiveness and springiness of gels increased with time and temperature. Gel microstructure consisted of spheres (4–50 μm) and granules (0.3–1.0 μm) dispersed in a continuous matrix. Spheres were physically disrupted by dilution and by addition of salt.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1987.tb13974.x
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  • 10
    Electronic Resource
    Electronic Resource
    Electrophoresis and Chromatography of Heat-Treated Plain, Sugared and Salted Whole Egg (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 48 (1983), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effects of heat treatments on the proteins in plain, 10% sugared and 10% salted whole egg were studied by polyacrylamide disc gel electrophoresis and diethylaminoethyl-Sephacel ion exchange chromatography. Electrophoretograms of products heated from 57–87°C for 3.5 min showed a wide range of protein stability. Livetins and some globulins were most heat sensitive, while conalbumin and ovalbumin were most stable. Sugar and salt increased heat stability of proteins by 1.6 and 7.9°C, respectively. Heat sensitive proteins were most stabilized by sugar and salt. Heating whole egg and sugared whole egg changed the chromatograms substantially, while heating salted whole egg caused fewer changes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1983.tb10776.x
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