Gelation of Egg White Proteins as Affected by Combined Heating and Freezing

Xu, Jinquan; Shimoyamada, Makoto; Watanabe, Kenji

doi:10.1111/j.1365-2621.1997.tb15016.x

Cited by 11 publications

(12 citation statements)

References 21 publications

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“…Controlled heating in dry state of egg white (for example, 80°C for 5-10 days) was found to be effective to improve significantly functionalities such as gelling, emulsifying, and foaming properties and water holding capacity without any loss in solubility (Kato et al, 1989(Kato et al, , 1990aMine, 1996Mine, , 1997. We also showed that when the solutions of spray-dried (60-70°C) and then dry-stored (55-65°C, 3 days) egg whites were reheated at 60°C for several minutes, coagulation hardly occurred (Xu et al, 1997). This phenomenon was also found to be mainly attributable to changes of the egg white proteins occurring in the process of heating in the dry state.…”

Section: Introductionmentioning

confidence: 82%

Inhibiting Effects of Egg White Dry-Heated at 120 °C on Heat Aggregation and Coagulation of Egg White and Characteristics of Dry-Heated Egg White

Watanabe

Shimoyamada

1999

J. Agric. Food Chem.

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Dialyzed and freeze-dried egg white (FDEW) was dry-heated at 120 degrees C for up to 6 h. The inhibiting effects of the dry-heated egg white (DHEW) on the heat aggregation and coagulation of egg white (as 10% FDEW solution) and characteristics of the DHEW were examined. From the changes in turbidities and soluble protein contents of supernatant in various mixtures of 10% FDEW and DHEW solutions induced by heating (60 degrees C, 5 min), it was found that the inhibiting capacity increased with increases in the dry-heating time (DHT). The FDEW proteins were denatured with a mild conformational change (not secondary but tertiary structure) with the increase in DHT and aggregated partially. However, the more transparent solutions of DHEW containing soluble aggregates according to DHT were also obtained after heating. The transparency according to DHT came to be scarcely affected by the NaCl concentration and the dilution with diluents containing SDS, urea, and 2-mercaptoethanol. These findings suggest that the heat aggregations and coagulations of ovotransferrin and lysozyme in the FDEW were inhibited by their bindings with the soluble aggregates in DHEW.

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Section: Introductionmentioning

confidence: 82%

Inhibiting Effects of Egg White Dry-Heated at 120 °C on Heat Aggregation and Coagulation of Egg White and Characteristics of Dry-Heated Egg White

Watanabe

Shimoyamada

1999

J. Agric. Food Chem.

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“…The gel sheets were stained with a solution of 0.2% Coomassie Brilliant Blue R-250 in water/methanol/acetic acid (5:5:1, v/v/v) and destained by 7% acetic acid overnight. Sodium dodecyl sulfate (SDS)-PAGE in the presence and absence of 2-mercaptoethanol (2-ME) was carried out according to the method of Laemmli (1970) as described in the previous paper (Xu et al, 1997).…”

Section: Effects Of Cacl 2 and Ph At Dry-heating On Dhew Turbidity An...mentioning

confidence: 99%

“…In a previous study (Xu et al, 1997), we showed that when solutions of spray-dried (60-70 °C) and then heattreated egg white (55-65 °C, 3 days in a dry state to reduce microbial numbers) were reheated at 60 °C for various times, the insoluble materials in their solutions almost failed to form. Such a phenomenon was also found to be mainly attributable to changes in proteins occurring in the process of heating in a dry state.…”

Section: Introductionmentioning

confidence: 96%

Heat Aggregation of Dry-Heated Egg White and Its Inhibiting Effect on Heat Coagulation of Fresh Egg White

Shimoyamada

Watanabe

1998

J. Agric. Food Chem.

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The characteristics of dialyzed and freeze-dried egg white that was dry-heated under various conditions (70−125 °C, 0 min−6 h) were studied. The dry-heated egg whites (DHEWs, 120 °C) showed the formation of insoluble aggregates (coagula) within 50 min, turbid soluble ones (50 min−2 h), and transparent soluble ones (2−6 h) according to the dry-heating times when solubilized at 10% concentration (pH 7.4) and reheated at 60 °C for 3.5 min. A transparent DHEW solution without any coagula when reheated was obtained by using a shorter dry-heating time and elevating the dry-heating temperature. It was also found that NaCl suppressed the turbidity development of DHEW solution promoted by CaCl2. When 10% DHEW solutions (120 °C, >2 h) were mixed with fresh egg white at the ratio of 1:1 in volume and heated at 60 °C for 3.5 min, coagulum formations in their mixtures were inhibited. The patterns of native− and SDS−PAGEs and gel filtration suggest that soluble aggregates of ovalbumin formed in the dry-heating process inhibit the formation of ovotransferrin coagula. Keywords: Egg white; dry-heating; heat coagulation; soluble aggregate

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“…The proteins of whole blood plasma, serum and plasma fractions interacted with egg white proteins producing stronger gels (Howell & Lawrie, 1984). The aggregations of serum protein with egg white can occur during heating through the exchange reaction of sulfhydryl groups and disulfide bonds (Howell & Lawrie, 1984;Xu et al, 1997). The exchange reaction of free sulfhydryl groups of ovalbumin with disulfide bonds of serum proteins, especially serum albumin, occurred when a small quantity of egg white or ovalbumin was added to the serum and enhanced the gel strength.…”

Section: Resultsmentioning

confidence: 99%

Heat-Induced Gelation of Charcoal-Treated Serum Protein.

Hayakawa

2001

FSTR

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The gel strength of charcoal-treated bovine serum and porcine serum proteins at a concentration of 8% was determined with different concentrations of NaCl after heating at 80˚C for 15 min at pH 7.0. The charcoal treatment considerably enhanced the gel strength of porcine serum protein, and also improved gel strength of bovine serum protein at NaCl concentrations between 75 mM and 150 mM. The gel strength of commercial PSA and BSA and that of fractionated bovine and porcine proteins by ion-exchange chromatography were also determined at a constant NaCl concentration. With the charcoal treatment, the gel strength of fractions containing albumin increased, while that containing globulin decreased. The gel strength of charcoal-treated bovine serum and porcine serum remarkably increased by the addition of the egg white, ovalbumin and glutathione. The promotion of gel formation with glutathione and ovalbumin seemed to result from the interaction between sulfhydryl groups in glutathione and ovalbumin and intramolecular disulfide bonds in the serum protein, thereby resulting in the highly organized matrix.

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Gelation of Egg White Proteins as Affected by Combined Heating and Freezing

Cited by 11 publications

References 21 publications

Inhibiting Effects of Egg White Dry-Heated at 120 °C on Heat Aggregation and Coagulation of Egg White and Characteristics of Dry-Heated Egg White

Inhibiting Effects of Egg White Dry-Heated at 120 °C on Heat Aggregation and Coagulation of Egg White and Characteristics of Dry-Heated Egg White

Heat Aggregation of Dry-Heated Egg White and Its Inhibiting Effect on Heat Coagulation of Fresh Egg White

Heat-Induced Gelation of Charcoal-Treated Serum Protein.

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