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Ph Effect on Thermal Transition Temperature of Collagen
Author(s) -
HORGAN D.J.,
KURTH L.B.,
KUYPERS R.
Publication year - 1991
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1991.tb04734.x
Subject(s) - differential scanning calorimetry , chemistry , thermal , atmospheric temperature range , transition (genetics) , transition temperature , calorimetry , thermal analysis , thermodynamics , biochemistry , physics , superconductivity , quantum mechanics , gene
Differential scanning calorimetry (DSC) was used to measure the thermal transition temperature of bovine intramuscular and tendon collagen. Equilibration of the collagen in buffers in the pH range 4.25–7.40 resulted in a decline in transition temperature with decreasing pH. This was more pronounced in collagen with higher concentrations of aldimine crosslinks. We proposed that postmortem pH decline was responsible for the thermal transition temperature decline observed by other workers. Therefore, thermal transition temperature measurements must be performed on collagen samples that have been thoroughly equilibrated to a common pH if they are to be used as indices of structural changes.