Journal ArticleDOI
Differential scanning calorimetric study of collagen fibres swollen in aqueous neutral salt solutions.
Arthur Finch,D.A. Ledward +1 more
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The effect of various salts at pH 5.6 to 6.2 on the enthalpy, ΔHD, and temperature, TD, of denaturation of swollen bovine achilles tendon collagen was studied.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 1973-01-25. It has received 32 citations till now.read more
Citations
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Journal ArticleDOI
A differential scanning calorimetry analysis of the age-related changes in the thermal stability of rat skin collagen
TL;DR: It is concluded that heat-labile and heat-stable crosslinks account for a collagen thermal stabilization which can explain the delay of denaturation characterized by the third peak of DSC thermograms.
Journal ArticleDOI
Effect of hydration upon the thermal stability of tropocollagen and its dependence on the presence of neutral salts
TL;DR: The endotherm enthalpy changes ΔHD and temperatures TD of thermal denaturation of tropocollagen fibers were measured by DSC calorimetry as functions of water content and the effect of water uptake on theEnthalpy term is explained by water bridge formation within the collagen triple helix.
Book ChapterDOI
Thermal analysis of food proteins
C.-Y. Ma,V.R. Harwalkar +1 more
TL;DR: Differential scanning calorimetry (DSC) or differential thermal analysis (DTA) is a group of techniques in which a physical property of a substance is measured as function of temperature while the substance is subjected to a controlled temperature program.
Journal ArticleDOI
Effects of temperature on food proteins and its implications on functional properties.
Arun Kilara,Tawfik Sharkasi +1 more
TL;DR: This article surveys the knowledge in the area of protein structure and chemistry of denaturation prior to an indepth review of the effects of heat on soy, milk, and egg proteins and reviews the methods available to assess denaturation of proteins.
References
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Journal ArticleDOI
Shrinkage of collagen fibres: a differential scanning calorimetric study.
Arthur Finch,D.A. Ledward +1 more
TL;DR: It is concluded that hydrophobic bonds are a major factor in the stabilisation of collagen fibres after swelling in deionised water.
Journal ArticleDOI
Mechanism of Gelation of Gelatin. Influence of Certain Electrolytes on the Melting Points of Gels of Gelatin and Chemically Modified Gelatins.
Journal ArticleDOI
The Effect of Aqueous Salt Solutions on the Melting of Collagen and the Viscosity of Gelatin
David Puett,L. V. Rajagh +1 more
TL;DR: In this paper, the shrinkage temperature in solutions of different salt concentration (CS) is controlled by the amount of diluent in equilibrium swelling with the molten network, and the shape of TS vs CS curves can be represented by conventional theories valid for binary polymer diluents systems based on a lattice model with a single interaction parameter.
Journal ArticleDOI
Schrumpfungstemperaturen von kollagen in gemischen aus organischen lösungsmitteln und wasser
Von J. Schnell,H. Zahn +1 more
TL;DR: The shrinkage temperature (Ts) of collagen was determined in mixtures of water and organic solvents as discussed by the authors, which is correlated to the influence of hydrophobic interactions on the stabilisation of the collagen structure.
Related Papers (5)
Thermal conformational transformation of tropocollagen. I. Calorimetric study
Shrinkage of collagen fibres: a differential scanning calorimetric study.
Arthur Finch,D.A. Ledward +1 more