[Study of heat denaturation of collagen dispersions by a method of IR-spectroscopy].

Infrared spectroscopy was used to examine the kinetics of deuterium exchange in collagen films prepared from its 0.5% dispersions obtained from cattle tendons and healed at 25--100 degrees C for 30 min. The temperature relationships to the denaturation degree and time of deuterium exchange suggested that an almost complete heat denaturation of dispersions can be achieved at 31.5 degrees C. The temperature of semi-denaturation of dispersions was 28.5--29.0 degrees. The occurrence of intact supermolecular aggregates of collagen molecules in its dispersions had no effect on the system resistance to heat denaturation.