Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis.
The dependence of the proton spin-lattice relaxation rate, and of the enthalpy and temperature of denaturation on water content, were studied by nmr and differential scanning calorimetry (DSC) in native and denatured collagen. Collagen was first heated at four different temperatures ranging from 40 to 70 degrees C. The percentage of denatured collagen induced by these preheating treatments was determined from DSC measurements. The DSC results are discussed in terms of heat-induced structural changes. A two-exponential behavior for the spin-lattice relaxation was observed with the appearance of denatured collagen. This was attributed to the presence of a noncollagen protein fraction. The variations in the different longitudinal relaxation rates as a function of the moisture content and of the denatured collagen percentage are described within the multiphase water proton exchange model. This study highlights the complementarity of the information obtained from the two analytical tools used.
Rochdi
A
A
Structures Tissulaires et Interactions Moléculaires, SRV INRA Theix, 63122 St Genès Champanelle, France.
Foucat
L
L
Renou
J P
JP
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy; D011489:Protein Denaturation; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
D014867:Water; D003094:Collagen