Determination of Cross‐link Density in Egg White Gels from Stress Relaxation Data

G. R. ZIEGLER; S. S.H. RIZVI

doi:10.1111/j.1365-2621.1989.tb08606.x

Determination of Cross‐link Density in Egg White Gels from Stress Relaxation Data

G. R. ZIEGLER, S. S.H. RIZVI

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18 Scopus citations

Abstract

The concentration of permanent cross‐links in egg white gels was determined using stress relaxation experiments and equations derived from the theory of rubber elasticity. Cross‐link densities of 1.2–1.3 covalent cross‐links/molecule were observed. The concentration of covalent cross‐links, most likely disulfide bonds, was only slightly higher for gels formed in water as compared to those formed in 0.6M NaCl‐0.2M phosphate buffer at pH 6.0. These results differ from the 3—4 cross‐links/molecule previously reported for ovalbumin gels in 0.6M urea.

Original language	English (US)
Pages (from-to)	218-219
Number of pages	2
Journal	Journal of Food Science
Volume	54
Issue number	1
DOIs	https://doi.org/10.1111/j.1365-2621.1989.tb08606.x
State	Published - Jan 1989

All Science Journal Classification (ASJC) codes

Food Science

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10.1111/j.1365-2621.1989.tb08606.x

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abstract = "The concentration of permanent cross‐links in egg white gels was determined using stress relaxation experiments and equations derived from the theory of rubber elasticity. Cross‐link densities of 1.2–1.3 covalent cross‐links/molecule were observed. The concentration of covalent cross‐links, most likely disulfide bonds, was only slightly higher for gels formed in water as compared to those formed in 0.6M NaCl‐0.2M phosphate buffer at pH 6.0. These results differ from the 3—4 cross‐links/molecule previously reported for ovalbumin gels in 0.6M urea.",

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year = "1989",

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AB - The concentration of permanent cross‐links in egg white gels was determined using stress relaxation experiments and equations derived from the theory of rubber elasticity. Cross‐link densities of 1.2–1.3 covalent cross‐links/molecule were observed. The concentration of covalent cross‐links, most likely disulfide bonds, was only slightly higher for gels formed in water as compared to those formed in 0.6M NaCl‐0.2M phosphate buffer at pH 6.0. These results differ from the 3—4 cross‐links/molecule previously reported for ovalbumin gels in 0.6M urea.

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Determination of Cross‐link Density in Egg White Gels from Stress Relaxation Data

Abstract

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