Heat Denaturation and Emulsifying Properties of Egg Yolk Phosvitin

Chung, Siew Lian; Ferrier, L.K.

doi:10.1111/j.1365-2621.1995.tb06258.x

Cited by 14 publications

(10 citation statements)

References 14 publications

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“…From this first series of observations, a feed concentration of 5.0% was chosen to concentrate PVs to have a reasonable permeate flux for concentration and desalting experiments at pH 8.0, under an operating pressure of 1.4 bar. Also, the operating temperature was set up at 50 °C, which is above the optimal temperature (30–35 °C) for microbial growth and below denaturation temperature of PVs ( T d = 79.7 ± 1.4 °C) (Chung & Ferrier, 1995). Moreover, a higher temperature is favourable to the membrane filtration because of the reduction in feed viscosity.…”

Section: Resultsmentioning

confidence: 99%

On the use of ultrafiltration for the concentration and desalting of phosvitin from egg yolk protein concentrate

Ting

Pouliot

Juneja

et al. 2010

Int J of Food Sci Tech

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An ultrafiltration-based approach was integrated in the preparation of phosvitin (PVs) from delipidated egg yolk proteins. An attempt was made to concentrate PVs as well as to desalt by means of the diafiltration technique. Primary experiments were devoted to optimise the ultrafiltration performance as function of parameters such as the effects of pH, feed concentration and transmembrane pressure on permeate flux with the 10-kDa molecular weight cut-off (MWCO) polyethersulfone membrane at laboratory scale. Higher permeate flux values were observed at low concentration and at alkaline pH, whatever transmembrane pressure studied. Then, desalting of PVs was carried out at 50°C with 10-and 30-kDa MWCO membranes. The results showed that desalting of PVs was obtained with both the 10-and 30-kDa MWCO membranes and with a few loss of protein in the permeate side.

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Section: Resultsmentioning

confidence: 99%

On the use of ultrafiltration for the concentration and desalting of phosvitin from egg yolk protein concentrate

Ting

Pouliot

Juneja

et al. 2010

Int J of Food Sci Tech

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show abstract

“…This is in agreement with Lu and Baker (1986), who observed similar effects on the antioxidant activity of phosvitin under autoclave conditions. The fact that phosvitin lost less than 15% of its ability to inhibit ironpromoted oxidation over the temperature range of 70 to 100°C was somewhat surprising since Chung and Ferrier (1995) reported a phosvitin denaturation temperature of 79.7 ± 1.4°C as determined by differential scanning calorimetry (phosvitin was in water at pH 7 and was heated at 10°C/ min). These data suggest that denatured phosvitin retains some of its ability to bind iron, which is in agreement with Albright and others (1984), who reported that heating whole egg or egg yolk for 20 or 40 min at 110°C did not result in the release of phosvitin-bound iron.…”

Section: Influence Of Heat Processing On the Antioxidant Activity Of mentioning

confidence: 99%

Antioxidant Activity of Phosvitin in Phosphatidylcholine Liposomes and Meat Model Systems

Lee¹,

Han²,

Decker³

2002

Journal of Food Science

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Phosvitin, an iron-chelating protein, was tested for its ability to inhibit lipid oxidation in phosphatidylcholine (PC) liposomes and meats. Inhibition of thiobarbituric acid reactive substances (TBARS) formation increased with increasing phosvitin concentrations with maximal inhibition occurring at 40 and 15 mM in PC liposomes and pork muscle homogenates, respectively. Phosvitin lost only 2 to 15% of its antioxidant activity after being heated for 10 min at 60 to 100 °C. The ability of phosvitin to inhibit TBARS formation was maximal at pH 7.0. Phosvitin was a more effective antioxidant in cooked ground pork with 20 mM inhibiting 11 to 39% of oxidation compared with 0 to 20% inhibition in uncooked, salted ground pork containing 60 mM phosvitin.

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“…The left-hand peak corresponds to the denaturation of ovotransferrin, the middle peak to that of lysozyme, and the peak at 84.1°C to that of ovalbumin (Van der Plancken et al, 2005a). On the other hand, there was a major endothermic peak (80.9°C) corresponding to the denaturation of phosvitin in egg yolk (Chung and Ferrier, 1995).…”

Section: Enthalpy Of Denaturationmentioning

confidence: 96%

Changes in physicochemical properties of egg white and yolk proteins from duck shell eggs due to hydrostatic pressure treatment

et al. 2010

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The shell of the duck egg did not crack after pressure treatments (300 to 500 MPa; 25 degrees C; 10 min) in this study; therefore, the changes of physicochemical properties of egg white and yolk proteins from the intact shell egg by pressure treatment were first investigated and compared with those of pressurized hen liquid eggs. Although the proximate compositions of duck eggs and hen eggs were similar, the moisture and protein contents of hen whole eggs were higher than those of duck whole eggs. The protein contents of duck egg white and yolk were slightly lower than those of hen eggs, and the moisture content of duck egg white was equal to that of hen egg white, whereas that of duck egg yolk was lower than that of hen egg yolk. After pressure treatment at 500 MPa, the results of solubility, sulfhydryl content, surface hydrophobicity, and residual denaturation enthalpy showed that egg white proteins underwent slight but significant unfolding and aggregation, whereas pressure treatments below 500 MPa induced insignificant changes in the physicochemical properties. On the other hand, pressure treatments at 400 and 500 MPa significantly reduced the solubility and residual denaturation enthalpy of egg yolk proteins. However, the native PAGE result showed that pressure treatment up to 500 MPa did not affect the protein components of egg white and yolk. The results showed that the application of pressure treatment on duck shell egg may induce reversible denaturation of both egg white and yolk proteins. The egg white and yolk proteins may be prevented from denaturation after pressure treatment in the presence of the eggshell compared with the absence of the eggshell. As reported in the literature, pressure treatments at 300 to 500 MPa and 25 degrees C would be efficient for decontamination of duck shell eggs. Therefore, based on the consideration for food safety and functional properties, pressure processing can be a good preservation technique for duck shell eggs.

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Heat Denaturation and Emulsifying Properties of Egg Yolk Phosvitin

Cited by 14 publications

References 14 publications

On the use of ultrafiltration for the concentration and desalting of phosvitin from egg yolk protein concentrate

On the use of ultrafiltration for the concentration and desalting of phosvitin from egg yolk protein concentrate

Antioxidant Activity of Phosvitin in Phosphatidylcholine Liposomes and Meat Model Systems

Changes in physicochemical properties of egg white and yolk proteins from duck shell eggs due to hydrostatic pressure treatment

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