Physicochemical and Functional Properties of Dehydrated Japanese Quail (Coturnix japonica) Egg White

Abstract

Physicochemical, functional and digestibility analyses were done of dehydrated quail egg white to determine its possible practical applications. Quail egg white was dehydrated by air convection using one of two temperatures and times: M1 (65, 3.5 h), M2 (65, 5.0 h), M3 (70, 3.5 h) and M4 (70, 5.0 h). Lyophilized quail egg white was used as a standard. All four air-dried treatments had good protein levels (92.56% to 93.96%), with electrophoresis showing the predominant proteins to be lysozyme, ovalbumin and ovotransferin. Denaturation temperatures ranged from 81.16 to 83.85 and denaturation enthalpy values from 5.51 to 9.08 J/g. Treatments M1-4 had lower water-holding (0.90 - 2.95 g/g) and oil-holding (0.92 - 1.01 g/g) capacities than the lyophilized treatment (4.5 g/g, 1.95 g/g, respectively). Foaming capacity was pH-dependent in all five treatments, with the lowest values at alkaline pH and the highest (153% to 222%) at acid pH (pH 2). Foam stability was lowest at acid pH and highest at alkaline pH. Emulsifying activity in the air-dried treatments was highest at pH 8 (41% - 46%). Emulsion stability was pH-dependent and highest in M3 between pH 2 and 4 (96.16% to 95.74%, respectively). In the air-dried treatments, in vitro protein digestibility was as high as 83.02% (M3).

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M. Segura-Campos, R. Pérez-Hernández, L. Chel-Guerrero, A. Castellanos-Ruelas, S. Gallegos-Tintoré and D. Betancur-Ancona, "Physicochemical and Functional Properties of Dehydrated Japanese Quail (Coturnix japonica) Egg White," Food and Nutrition Sciences, Vol. 4 No. 3, 2013, pp. 289-298. doi: 10.4236/fns.2013.43039.

Conflicts of Interest

The authors declare no conflicts of interest.

References

[1] N. Vali, “The Japanese Quail: A Review,” International Journal of Poultry Science, Vol. 7, No. 9, 2008, pp. 925-931. doi:10.3923/ijps.2008.925.931
[2] B. B. Kayang, A. Vignal, M. Inoue-Murayama, M. Miwa, J. L. Monvoisin, S. Ito and F. Minvielle, “A First-Generation Micro Satellite Linkage Map of the Japanese Quail,” Animal Genetics, Vol. 35, No. 3, 2004, pp. 195-200. doi:10.1111/j.1365-2052.2004.01135.x
[3] J. K. Amoah and E. A. Martin, “Quail (Coturnix coturnix japonica) Layer Diets Based on Rice Bran and Total or Digestible Amino Acids,” Journal of Applied Bioscience, Vol. 26, No. 2, 2010, pp. 1647-1652.
[4] M. González, “Influence of Age on Physical Traits of Japanese Quail (Coturnix coturnix japonica) Eggs,” Animal Research, Vol. 44, No. 3, 1995, pp. 307-312. doi:10.1051/animres:19950309
[5] D. Cardoso-Jiménez, S. Rebollar-Rebollar, R. Rojo-Rubio, “Productivity and Profitability of the Quail (Coturnix coturnix japonica) in the Southern Region of the State of Mexico,” Mexican Journal of Agronomy, Vol. 12, No. 22, 2008, pp. 517-525.
[6] A. C. Carraro-Alleoni, “Albumen Protein and Functional Properties of Gelation and Foaming,” Science Agriculture, Vol. 63, No. 3, 2006, pp. 291-298.
[7] W. Horwitz, “Official Methods of Analysis,” 17th Edition, Association of Official Analytical Chemists, Washington DC, 1997.
[8] H. Schagger and G. Von Jagow. “Tricine-Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis for the Separation of Proteins in the Range from 1 to 100 kDa,” Analytical Biochemistry, Vol. 166, No. 2, 1987, pp. 368-379. doi:10.1016/0003-2697(87)90587-2
[9] E. N. Martínez and M. C. Anon, “Composition and Structural Characterization of Amaranth Protein Isolates. An Electrophoretic and Calorimetric Study,” Journal of Agricultural and Food Chemistry, Vol. 44, No. 9, 1996, pp. 2523-2530. doi:10.1021/jf960169p
[10] L. Chel-Guerrero,V. Pérez-Flores, D. Betancur-Ancona and G. Dávila-Ortiz, “Functional Properties of Flours and Protein Isolates from Phaseolus lunatus and Canavalia ensiformis Seeds,” Journal of Agricultural and Food Chemistry, Vol. 50, No. 3, 2002, pp. 584-591. doi:10.1021/jf010778j
[11] H. Hsu, D. Vavak, L. Satterlee and G. Miller, “A Multi Enzyme Technique for Estimating Protein Digestibility,” Journal of Food Science, Vol. 42, No. 5, 1977, pp. 1269-1279. doi:10.1111/j.1365-2621.1977.tb14476.x
[12] D. Montgomery, “Diseno y Análisis de Experimentos,” Limusa-Wiley, México DF, 2004.?
[13] I. O. Dudusola, “Comparative Evaluation of Internal and External Qualities of Eggs from Quail and Guinea Fowl,” International Research Journal of Plant Science, Vol. 1, No. 5, pp. 112-115.
[14] C. V. Morr, B. German, J. E. Kinsella, J. M. Regenstein, J. P. Van Buren, A. Kilara, B. A. Lewis and M. E. Mangino, “A Collaborative Study to Develop a Standardized Food Protein Solubility Procedure,” Journal of Food Science, Vol. 50, No. 6, 1985, pp. 1715-1718. doi:10.1111/j.1365-2621.1985.tb10572.x
[15] A. Baniel, A. Fains and Y. Popineau, “Foaming Properties of Egg Albumen with a Bubbling Apparatus Compared with Whipping,” Journal of Food Science, Vol. 62, No. 2, 1997, pp. 377-381. doi:10.1111/j.1365-2621.1997.tb04005.x
[16] B. Vani and J. F. Zayas, “Foaming Properties of Selected Plant and Animal Proteins,” Journal of Food Science, Vol. 60, No. 5, 1995, pp. 1025-1028. doi:10.1111/j.1365-2621.1995.tb06285.x
[17] I. Boni, H. Nurul and I. Noryati, “Comparison of Meat Quality Characteristics between Young and Spent Quails,” International Food Research Journal, Vol. 17, No. 3, 2010, pp. 661-666.
[18] W. I. Stadelman and O. J. Cotterill, “Foaming,” In: Egg Science & Technology, Food Product Press, Haworth Press Inc., Binghamton, 1994, pp. 418-434.
[19] T. Matsuda, K. Watanabe and Y. Sato, “Heat-Induced Aggregation of Egg White Proteins as Studied by Vertical Flat-Sheet Polyacrylamide Gel Electrophoresis,” Journal of Food Science, Vol. 46, No. 6, 1981, pp. 1829-1834. doi:10.1111/j.1365-2621.1981.tb04498.x
[20] M. ?. Raeker and L. A. Johnson, “Thermal and Functional Properties of Bovine Blood Plasma and Egg White Proteins,” Journal of Food Science, Vol. 60, No. 4, 1995, pp. 685-690. doi:10.1111/j.1365-2621.1995.tb06206.x
[21] C. Myers, “Study of Thermodynamics and Kinetics of Protein Stability by Thermal Analysis,” In: Thermal Analysis of Foods, Elsevier Science Publishing Co., Inc., New York, 1990, pp. 16-50.
[22] J. C. Cheftel, J. L. Cuq and D. Lorient, “Proteínas Alimentarias,” Acribia, Zaragoza, 1989, pp. 49-175.
[23] R. J. Kanterewicz, B. E. De Elizalde, A. M. R. Pilosof and G. B. Bartholomai, “Water-Oil Absorption Index (WOAI): A Simple Method for Predicting the Emulsifying Capacity of Food Proteins,” Journal of Food Science, Vol. 52, No. 5, 1987, pp. 1381-1383. doi:10.1111/j.1365-2621.1987.tb14087.x
[24] L. Du, A. Prokop and R. D. Tanner, “Effect of Denaturation by Preheating on the Foam Fractionation Behavior of Ovalbumin,” Journal of Colloid and Interface Science, Vol. 248, No. 2, 2002, pp. 487-492. doi:10.1006/jcis.2001.8163
[25] J. B. German and L. Phillips, “Protein Interactions in Foams: Protein-Gas Phase Interactions,” In: Protein Functionality in Food Systems, Marcel Dekker, Inc., New York, 1994, pp. 181-208.
[26] E. Doi and N. Kitabatake, “Structure and Functionality of Egg Proteins,” In: Food Proteins and Their Applications, Marcel Dekker, Inc., New York, 1997, pp. 325-340.
[27] E. Li-Chan and S. Nakai, “Raman Spectroscopy Study of Thermally and/or Dithiothreitol Induced Gelation of Lisozyme,” Journal of Agricultural and Food Chemistry, Vol. 39, No. 7, 1991, pp. 1238-1245. doi:10.1021/jf00007a009
[28] M. Ahmenda, W. Prinyawiwatkul and R. Rao, “Solubilized Wheat Protein Isolate: Functional Properties and Potential Food Applications,” Journal of Agricultural and Food Chemistry, Vol. 47, No. 4, 1999, pp. 1340-1345. doi:10.1021/jf981098s
[29] C. F. Chau, K. Cheung and Y. S. Wong, “Functional Properties of Protein Concentrates from Three Chinese Indigenous Legume Seeds,” Journal of Agricultural and Food Chemistry, Vol. 45, No. 11, 1997, pp. 2500-2503. doi:10.1021/jf970047c
[30] C. R. Hank, M. E. Kunkel, P. L. Dawson, J. C. Acton and F. B. Wardlaw, “The Effect of the Shell Egg Pasteurization on the Protein Quality of Albumen,” Poultry Science, Vol. 80, No. 6, 2001, pp. 821-824.

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