Density Variation in Heat- and Pressure-Treated Egg White during Gel-to-Glass-like Transition

Kanaya, Haruichi; Ishida, Kenji; Hara, Kazuhiro; Okabe, Hirotaka; Taki, Seiji; Matsushige, Kazumi; Takushi, Eisei

doi:10.1143/jjap.31.3754

Cited by 22 publications

(1 citation statement)

References 36 publications

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“…For example, the effect of hydration on the density of water and alcohol mixture is not negligible, since the total volume decreases with mixing. In the present case, Kanaya et al measured volume and weight of the boiled egg white and reported that the density of the boiled egg white does not change much (1.0–1.2 g/cm 3 ) during the gel–glass transition 50. Therefore, it is reasonable that C P and C W were determined by only the ratio of the protein and water content as described in Eqs.…”

Section: Methodsmentioning

confidence: 71%

Globule-coil transition of denatured globular protein investigated by a microwave dielectric technique

Hayashi¹,

Miura²,

Shinyashiki³

et al. 2000

Biopolymers

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A mechanism for the gel–glass transition of denatured globular protein has been explained from the viewpoint of the globule–coil transition with microwave dielectric measurements using a time domain reflectometry (TDR) method. Boiled egg white, which is an aqueous gel of egg white prepared by heat treatment at 100°C, becomes a glass on drying. In the gel state, the relaxation processes corresponding to the orientation of bulk water and the micro‐Brownian motion of peptide chains of denatured protein were observed around 10 GHz and 10 MHz, respectively. When the gel–glass transition occurred, the relaxation strength for bulk water decreased rapidly as evaporation and breaking of water structure occurred. Simultaneously, the relaxation strength for micro‐Brownian motion increased abruptly, as the structure of globular protein varied from globule state to coiled state. It is considered that the protein molecule spreads out and takes up a coiled state by reductions of hydrophobic and hydrophilic interactions of the globular protein. These reductions occur through a decrease in the amount of water. © 2000 John Wiley & Sons, Inc. Biopoly 54: 388–397, 2000

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Section: Methodsmentioning

confidence: 71%