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

M. L. LAMBRI; P. B. BOZZANO; E. D. GIORDANO; D. GARGICEVICH; J. I. PÉREZ-LANDAZÁBAL; F. G. BONIFACICH; G. I. ZELADA; V. RECARTE; O. A. LAMBRI

Córdoba

Congreso; Congreso SAM-CONAMET-IBEROMAT 2016; 2016

Thethermal stability of type I collagen from cow bones, either femur and ribs, wasstudied in the temperature range from 250 K up to 670 K by means of dynamicmechanical analysis, scanning electron microscopy and infrared absorptionspectroscopy. Several stages of denaturation were found in the temperaturerange from 320 K up to 670 K. Dynamic mechanical analysis, scanning electronmicroscopy and infrared absorption studies reveal the denaturation processeswhich take place at the collagen including also the triple helix towards therandom coil transition of the collagen fibrils.Thedifferences between the denaturation process in the femur and ribs arehighlighted and the physical-chemical mechanisms controlling the denaturationprocesses are discussed.