Eggs as a source of protein

Vadehra, D. V.; Nath, Kamalendu; Forsythe, Richard H.

doi:10.1080/10408397309527158

Cited by 95 publications

(50 citation statements)

References 693 publications

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“…Osuga & Feeney (1977) observed that ovomucoid from poultry eggs inhibits the bovine trypsin but not the human trypsin. Ovomucoid's molecular weight varies from 26,100 to 28,300 Da, and its isoelectric point lies between 3.9 and 4.3 (Vadehra & Nath, 1973). This protein is stabilized by hydrophobic strengths and its high resistance to heat results from its high cystine contents and, consequently, to the high number of disulphide linkages -eight (Vadehra & Nath, 1973).…”

Section: Ovomucoidmentioning

confidence: 99%

“…The eggwhite has two forms of ovomucin; the insoluble form characterizes the high viscosity of eggwhite's thin layer (Hayakawa & Sato, 1977). Ovomucin presents from one to 2% of eggwhite's total proteins (Vadehra & Nath, 1973), and differs from other proteins because its molecule is extremely large and Powrie & Nakai, 1985).…”

Section: Ovomucinmentioning

confidence: 99%

“…Ovomucin's molecular weight varies from 5.5 to 8.3 MDa. Ovomucin also has a substantial amount of disulphide groups, and up to 33% carbohydrates (Vadehra & Nath, 1973).…”

Section: Ovomucinmentioning

confidence: 99%

“…S-ovalbumin has a slightly lighter molecular weight than ovalbumin and its relative quantity in the eggwhite can increase during the storage period, from 5% in fresh eggs to 81% after six months of refrigerated storage. Both pH and temperature also affect the s-albumin formation (Vadehra & Nath, 1973). The sovalbumin dependency on pH indicates a step of initial ionization involving a sulphydrilic group and an amino group, or even the dependency on the concentration of hydroxyl ion, similar to an alkaline hydrolysis (Smith & Back, 1965).…”

mentioning

confidence: 99%

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Albumen protein and functional properties of gelation and foaming

Alleoni¹

2006

Sci. agric. (Piracicaba, Braz.)

134

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Hen eggwhite proteins have been extensively utilized as ingredients in food processing because of their unique functional properties, such as gelling and foaming. This work reviews the molecular basis of the eggwhite proteins targeting the development of these functional properties during processing. Key words: ovalbumin, coagulation, gel, denaturation PROTEÍNAS DO ALBUME E PROPRIEDADES FUCIONAIS DE GELATINIZAÇÃO E FORMAÇÃO DE ESPUMARESUMO: As proteínas da clara do ovo de galinha têm sido extensivamente usadas como ingredientes em alimentos processados, devido às suas propriedades funcionais, tais como gelatinização e formação de espuma. Essa revisão aborda as bases moleculares das proteínas da clara do ovo para o desenvolvimento dessas propriedades funcionais durante o processamento.

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Section: Ovomucoidmentioning

confidence: 99%

Section: Ovomucinmentioning

confidence: 99%

“…Ovomucin's molecular weight varies from 5.5 to 8.3 MDa. Ovomucin also has a substantial amount of disulphide groups, and up to 33% carbohydrates (Vadehra & Nath, 1973).…”

Section: Ovomucinmentioning

confidence: 99%

mentioning

confidence: 99%

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Albumen protein and functional properties of gelation and foaming

Alleoni¹

2006

Sci. agric. (Piracicaba, Braz.)

134

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“…Some reports have suggested that there are in excess of 40 proteins in EW. 5,6) To date, many minor proteins have not been identified. [7][8][9][10] Among the referenced proteins in avian EW, most are acidic proteins, having pI < 7, while only two are identified as basic proteins, proteins that have pI > 7, lysozyme (pI ¼ 10:7) and avidin (pI ¼ 10).…”

mentioning

confidence: 99%

Structural and Physicochemical Characteristics of Novel Basic Proteins Isolated from Duck Egg White

Naknukool

Hayakawa

Sun

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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Novel basic proteins, duck basic protein small 1 (dBPS 1 ) and 2 (dBPS 2 ), were isolated from duck egg white by cation-exchange and gel filtration chromatography. Protein sequence analyses indicated that they possessed 39 amino acid residues with three disulfide bonds. The amino acid sequence of dBPS 1 showed 45% identity with dBPS 2 . The amino acid sequence of dBPS 2 was the same as cygnin, a small protein from black swan, and strongly homologous with meleagrin from turkey and chicken. Phylogenic relationships implied that dBPS 1 and dBPS 2 share a common ancestry with cygnin and meleagrin. Based on MALDI-TOF mass spectra, the molecular masses of dBPS 1 and dBPS 2 were 4,373, and the 4,486 Da. pI of dBPS 1 and dBPS 2 elucidated by isoelectric focusing were 9.35 and 9.44. FT-IR spectra classified these proteins as ( ) proteins. Both dBPS 1 and dBPS 2 , possessed high heat stability, Td 101.2 and 98.3 C. Indirect ELISA results showed that the dBPS 1 /dBPS 2 -related proteins were distributed in the oviduct and gallbladder.

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Influence of pH on surface properties of aqueous egg albumen solutions in relation to foaming behaviour

Hammershøj¹,

Prins

Qvist

1999

J. Sci. Food Agric.

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The surface properties of aqueous egg albumen protein solutions (0.1 g litre−1) were studied at pH values of 4.8, 7.0, 9.2 and 10.7 and related to foaming behaviour such as bubble size distribution, overrun and drainage. By measurements far from equilibrium of dynamic steady state surface dilation using the overflowing cylinder technique, egg albumen showed ability to slow down surface expansion and to lower the dynamic surface tension. The pH‐effect was small, but at pH 4.8 the film length, at which a motionless surface was created, was longer than at higher pH indicating a somewhat more rigid surface at low pH. Near equilibrium sinusoidal surface area deformation resulted in relatively high moduli of egg albumen, with a significant effect of pH. The surface modulus E showed at pH 4.8 an increase in the course of time, but at higher pH it was constant. Large deformation of egg albumen surface was not destructive, and for all pH values the surface behaved viscoelastic, with highest loss modulus E″ and tan θ values at pH 4.8. Surface deformation frequency sweeps revealed the relaxation processes to be relatively slow at pH 4.8 and faster at pH 7.0–10.7. Foamability measured as overrun of foam as a result of shaking and stirring was highest at pH 4.8 and lowest at pH 10.7. Foam stability against drainage was best at pH 7.0 after 30 min, but at a long‐term scale foam at pH 4.8 was most resistant to drainage. Foam samples were subjected to microscopy and image analysis. The smallest bubbles were found at pH 4.8 (mean diameter 142 µm) and the largest at pH 7.0 (mean diameter 328 µm). In conclusion, the foaming behaviour of an aqueous egg albumen solution at pH 4.8 can be related to dynamic surface properties as follows: the more rigid behaviour of the surface at this pH favours a small bubble size and slow drainage of liquid from the foam. The high overrun at this pH can be explained by a lower dynamic surface tension, but also here film stability during foam making can be promoted by a more rigid liquid surface. © 1999 Society of Chemical Industry

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Eggs as a source of protein

Cited by 95 publications

References 693 publications

Albumen protein and functional properties of gelation and foaming

Albumen protein and functional properties of gelation and foaming

Structural and Physicochemical Characteristics of Novel Basic Proteins Isolated from Duck Egg White

Influence of pH on surface properties of aqueous egg albumen solutions in relation to foaming behaviour

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