DENATURATION PROCESSES OF COLLAGEN FROM COW BONES AS A FUNCTION OF TEMPERATURE

MELANIA L. LAMBRI; PATRICIA B. BOZZANO; ENRIQUE D. V. GIORDANO; DAMIÁN GARGICEVICH; J. I. PÉREZ-LANDAZÁBAL; FEDERICO GUILLERMO BONIFACICH; GRISELDA I. ZELADA; VICENTE RECARTE; OSVALDO AGUSTÍN LAMBRI

Córdoba

Congreso; Congreso Internacional de Metalurgia y Materiales; 2016

SAM - Asociación Argentina de Materiales

The thermal stability of type I collagen from cow bones, either femur and ribs, was studied in the temperature range from 250 K up to 670 K by means of dynamic mechanical analysis, scanning electron microscopy and infrared absorption spectroscopy. Several stages of denaturation were found in the temperature range from 320 K up to 670 K. Dynamic mechanical analysis, scanning electron microscopy and infrared absorption studies reveal the denaturation processes which take place at the collagen including also the triple helix towards the random coil transition of the collagen fibrils.The differences between the denaturation process in the femur and ribs are highlighted and the physical-chemical mechanisms controlling the denaturation processes are discussed.