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Determination of the number of cross‐links in a protein gel from its mechanical and swelling properties
Author(s) -
Van Kleef F. S. M.,
Boskamp J. V.,
Van Den Tempel M.
Publication year - 1978
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1978.360170118
Subject(s) - rubber elasticity , chemistry , ovalbumin , swelling , shear modulus , dynamic mechanical analysis , viscoelasticity , molecule , thermodynamics , solvent , natural rubber , polymer , chemical engineering , polymer chemistry , composite material , materials science , organic chemistry , physics , immune system , engineering , immunology , biology
The relation between the chemical structure of a protein and the physical properties of a heat‐set gel of that protein has been investigated. The physical properties of the gel are determined by means of mechanical experiments in which the viscoelastic properties of the gel are determined in terms of the storage shear modulus, the loss modulus and the stress‐strain curve. The storage shear modulus defined the solid (elastic) character of the gel. The chemical structure of the protein and the nature of the solvent determine the nature and number of cross‐links in the gel. The cross‐links in gels formed by heating concentrated solutions of ovalbumin in 6 M urea solutions were found to be disulfide bridges and the mechanical properties of these ovalbumin/urea gels approximated those of an ideal rubber. The latter finding enables one to calculate the number of cross‐links per ovalbumin molecule from the value of the storage modulus, using the classical theory of rubber elasticity. This theory, together with the Flory‐Huggins lattice model, can also be used to calculate the number of cros‐links per ovalbumin molecule from the swelling behavior of ovalbumin/urea gels. The number of cross‐links per ovalbumin molecule calculated from these two types of experiments are in mutual agreement and correspond with the number of thiol groups in ovalbumin. We conclude, thereforee, that theories of polymer physics can be used to relate the chemical structure of a protein to the physical properties of its gel.