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.

has been cited by the following article:

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

  AUTHORS: Maira Segura-Campos, Roberto Pérez-Hernández, Luis Chel-Guerrero, Arturo Castellanos-Ruelas, Santiago Gallegos-Tintoré, David Betancur-Ancona

  KEYWORDS: Coturnix japonica; Dehydrated Egg White; Physicochemical Properties; Functional Properties

  JOURNAL NAME: Food and Nutrition Sciences, Vol.4 No.3, March 19, 2013

  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).