To characterize the thermal denaturation behavior of solubilized collagen solution, the temperature dependence of the helix fraction (
X) and the differentiated curve (d
X/d
T) of X established by optical rotation measurements were investigated. On the d
X/d
T curve of the pepsin-solubilized collagen (PC1) solution, the small thermal denaturation peak (component L) was found at a lower temperature (
TL) along with the main thermal denaturation peak (component H) at a higher temperature (
TH). Thus, the effects of experimental conditions on
TL,
TH, and the ratio (L/H) of the amount of component L to that of component H were examined. The effects of the heating rate and the concentration of collagen on
TL and
TH were small.
TH decreased with the increase of the concentration of acetic acid or sodium chloride, and reached minimum at pH 3.5 to 4.5. L/H ratio was unchanged. However, as the irradiation time of ultraviolet rays increased,
TL and T
Hdecreased slightly and L/H increased. For commercially available collagens and solubilized collagens prepared from hides, the thermal denaturation behavior of their solutions and their patterns of the sodium dodecyl sulphate-polyacrylamide gel slab electrophoresis (SDS-PAGE) indicated that collagens, with large L/H values, had many bands without sub-units. The component L of each collagen was probably damaged due to crushing and solubilization.
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