Egg White Proteins (egg + white_protein)

Distribution by Scientific Domains


Selected Abstracts


COMPARATIVE STUDY OF EGG WHITE PROTEIN AND EGG ALTERNATIVES USED IN AN ANGEL FOOD CAKE SYSTEM

JOURNAL OF FOOD PROCESSING AND PRESERVATION, Issue 2010
MAHMOUD ABU-GHOUSH
ABSTRACT Comparisons of the physical and sensory properties of several commercial egg alternatives in angel food cake formulation were studied. Fourteen samples were investigated for foaming properties at 10 and 20 min whipping time: collagen, Cryogel gelatin, Solugel collagen hydroysates, gelatin, whey protein concentrate, fish protein, whey protein isolate (95% WPI, 90%WPI), hydrolyzed whey protein isolate, pea protein, rice protein concentrate, soy protein, corn zein and casein. However, only eight samples showed potential and were moved forward for further evaluation. Only the WPI alternative was able to maintain a meringue during baking. All other foams collapsed during the baking process. The angel food cake formulated with WPI exhibited a significantly firmer crust and crumb compared with the egg white control. The L value, height and volume of control cake were also significantly higher than the egg alternative. The control significantly outperformed the angel food cake formulated with the egg alternative in all sensory categories evaluated. PRACTICAL APPLICATIONS The egg alternatives were used to replace egg as a functional ingredient in angel cake productions. These alternatives can deliver functionality at a lower cost and can be incorporated to produce a suitable angle cake, especially whey protein isolate (WPI). These results may help producers in formulating angle cake that rely on WPI as an egg alternative. [source]


Qualification and Quantification of Fish Protein in Prepared Surimi Crabstick

JOURNAL OF FOOD SCIENCE, Issue 5 2008
Z.H. Reed
ABSTRACT:, Species identification and protein quantification in surimi crabstick were achieved using sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE). When the Lowry and Kjeldahl protein determination methods were compared, the former showed more consistent results. Densitometric scanning of the gels was used for quantification of total fish protein as well as total egg white protein. The lower molecular weight proteins, 30 kDa and lower, proved to be the most useful in fish species identification as well as egg white protein addition. Using a combination of the myosin heavy chain band and the species-specific myosin light chain (Alaska pollock: 22.5 kDa; Pacific whiting: 24.4 kDa) proved the most accurate in calculating fish protein content of the crabstick sample, while for those samples that contained egg white, quantification was accomplished from the densitometric analysis of the overlapping bands of actin (45 kDa) from fish and ovalbumin from egg white. Lysozyme (14.3 kDa) proved to be a unique protein band in determining the presence of egg white when the content of dried egg white was equal to or exceeded 0.5% of the total weight of the final crabstick. [source]


A convenient and sensitive allergy test: IgE crosslinking-induced luciferase expression in cultured mast cells

ALLERGY, Issue 10 2010
R. Nakamura
To cite this article: Nakamura R, Uchida Y, Higuchi M, Nakamura R, Tsuge I, Urisu A, Teshima R. A convenient and sensitive allergy test: IgE crosslinking,induced luciferase expression in cultured mast cells. Allergy 2010; 65: 1266,1273. Abstract Background:, For the detection of allergen-specific IgE in sera, solid-phase IgE-binding assays like the CAP test are commonly used. Although such immunochemical methods are very sensitive, they frequently produce false positives. Degranulation of the human IgE receptor (Fc,RI)-transfected rat mast cell (RBL) lines seems to be a possible indicator for human IgE, but spontaneous mediator release from these cells in the presence of human sera is not negligible. Methods:, The nuclear factor of activated T-cells (NFAT)-responsive luciferase reporter gene was stably transfected into human Fc,RI-expressing RBL-SX38 cells. One established clone (RS-ATL8) was sensitized with 1 : 100 dilution of sera from patients with egg white allergy and then stimulated with purified or a crude extract of egg white allergen. Results:, Sensitization with 15 pg/ml IgE was sufficient to detect IgE crosslinking,induced luciferase expression (EXiLE) by anti-IgE stimulation. Allergen-specific EXiLE was elicited by as little as 1 fg/ml of egg white protein without cytotoxicity. There was a good correlation between results with EXiLE and oral food challenge tests on patients with egg allergy (P = 0.001687, Fisher's exact test). The measured values of EXiLE and the CAP test also correlated well (R = 0.9127, Spearman's test). Conclusion:, The EXiLE test using RS-ATL8 cells is a promising in vitro IgE test to evaluate the biological activity of the binding between IgE and allergens. [source]


Partitioning of chicken egg white proteins in polyelectrolyte/salt aqueous two-phase systems composed of polyethyleneoxide,maleic acid copolymer and potassium phosphate

JOURNAL OF CHEMICAL TECHNOLOGY & BIOTECHNOLOGY, Issue 4 2002
Toshio Kajiuchi
Abstract Aqueous two-phase systems were formed from solutions of a polyelectrolyte, polyethyleneoxide,maleic acid copolymer, and potassium phosphate. The properties of such aqueous two-phase systems were highly dependent on pH. This was reflected in the partition behavior of three chicken egg white proteins: lysozyme, conalbumin and ovalbumin. Separability of these three proteins was improved by the use of the polyelectrolyte, in comparison with when uncharged polyethylene glycol (poly(1,2-dihydroxyethane)) was used as a phase-forming polymer. 2002 Society of Chemical Industry [source]


CHROMATOGRAPHIC SEPARATION AT A PREPARATIVE SCALE OF EGG WHITE OVALBUMIN AND ITS APPLICATION IN THE ELABORATION OF YOGURT MOUSSE

JOURNAL OF FOOD PROCESS ENGINEERING, Issue 1 2006
B. PAREDES
ABSTRACT Egg white contains high-quality proteins. Some processes using eggs produce egg white as by-product. These egg white proteins may be recovered for use as additive in food products. In the first part of this study, a new polymeric material was developed and used in the chromatographic separation of ovalbumin at preparative scale. Ovalbumin is the major component of egg white and thus, it has the greatest weight in terms of its functional effects. An application of the purified ovalbumin was subsequently studied in the elaboration of yogurt mousse. The results obtained showed that the poly(glycidil methacrylate-co-ethylene dimethacrylate) resin that was manufactured enabled the separation of ovalbumin with good efficiency. This study also showed that the formulation obtained from the yogurt mousse with ovalbumin had a greater yield in volume than the commercial product used as a benchmark, improving the majority of its organoleptic qualities without appreciably affecting its stability and organoleptic properties. [source]


State of the art and new horizons in the diagnosis and management of egg allergy

ALLERGY, Issue 3 2010
A. H. Benhamou
To cite this article: Benhamou AH, Caubet J-C, Eigenmann PA, Nowak-We,grzyn A, Marcos CP, Reche M, Urisu A. State of the art and new horizons in the diagnosis and management of egg allergy. Allergy 2010; 65: 283,289. Abstract Egg allergy is one of the most frequent food allergies in children below the age of three. Common symptoms of egg allergy involve frequently the skin as well as the gut and in more severe cases result in anaphylaxis. Non-IgE-mediated symptoms such as in eosinophilic diseases of the gut or egg-induced enterocolitis might also be observed. Sensitization to egg white proteins can be found in young children in absence of clinical symptoms. The diagnosis of egg allergy is based on the history, IgE tests as well as standardized food challenges. Ovomucoid is the major allergen of egg, and recent advances in technology have improved the diagnosis and follow-up of patients with egg allergy by using single allergens or allergens with modified allergenic properties. Today, the management of egg allergy is strict avoidance. However, oral tolerance induction protocols, in particular with egg proteins with reduced allergenic properties, are promising tools for inducing an increased level of tolerance in specific patients. [source]


Individual female clutch identification through yolk protein electrophoresis in the communally breeding guira cuckoo (Guira guira)

MOLECULAR ECOLOGY, Issue 11 2002
Mariana O. Cariello
Abstract Avian communal breeding systems generate alternative behavioural strategies for females, resulting in differences in reproductive success. Identifying eggs of different females in such systems is problematic, however, due to egg destruction before incubation, difficulty of capturing adults, and/or inaccuracy of egg identification based on egg morphometry. Here, we describe a technique that uses electrophoresis of yolk proteins to determine egg ownership, which we applied to communally breeding guira cuckoos (Guira guira). Validation of the method included identical yolk protein banding patterns in all eggs of the same female, but different patterns in eggs of different females in budgerigars (Melopsittacus undulatus), and identical patterns in yolk follicles of the same females in guira cuckoos. We applied the protocol to 195 guira cuckoo eggs from 34 joint nests in 2 years. All multiple guira cuckoo eggs laid on the same day in single nests had distinct banding patterns of yolk proteins, practically eliminating the possibility of more than one female being represented by the same pattern. Some identical banding patterns were repeated in different days within a nesting bout, indicating that some females laid several eggs in shared nests. Identical patterns occasionally occurred in renestings of groups, indicating that some females lay eggs in consecutive nestings. Yolk protein electrophoresis is a useful tool to identify egg maternity in other circumstances, such as polygynous mating systems with joint nests and intraspecific parasitism. Additionally, it is an alternative method for species where electrophoresis of egg white proteins does not show sufficient polymorphism. [source]