Non-isothermal kinetic analysis of the thermal denaturation of type I collagen in solution using isoconversional and multivariate non-linear regression methods

Published on Dec 1, 2010in Polymer Degradation and Stability5.03
· DOI :10.1016/J.POLYMDEGRADSTAB.2010.09.012
Wentao Liu17
Estimated H-index: 17
(Sichuan University),
Guoying Li22
Estimated H-index: 22
(Sichuan University)
Sources
Abstract
Abstract To further understand the kinetics of the thermal denaturation of type I collagen, the 16 and 8 mg/mL bovine hide collagen solutions were studied by differential scanning calorimetry at different heating rates. The activation energy of the denaturation process was examined utilizing the differential (Friedman) and the integral (Ozawa-Flynn-Wall) isoconversional methods, and several kinetic models were evaluated using the method of multivariate non-linear regression. Besides, the denaturation behavior was simulated under different temperature conditions. Results showed that the activation energy decreased in a different way at lower and higher degrees of conversion, respectively. A three-state model, in which a reversible step was followed by an irreversible one, was the best of the estimated models to describe the denaturation process, which could be approximated by single-step or two-consecutive-step in terms of temperature conditions.
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References33
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#1Matthew D. Shoulders (UW: University of Wisconsin-Madison)H-Index: 20
#2Ronald T. Raines (UW: University of Wisconsin-Madison)H-Index: 102
Collagen is the most abundant protein in animals. This fibrous, structural protein comprises a right-handed bundle of three parallel, left-handed polyproline II-type helices. Much progress has been made in elucidating the structure of collagen triple helices and the physicochemical basis for their stability. New evidence demonstrates that stereoelectronic effects and preorganization play a key role in that stability. The fibrillar structure of type I collagen—the prototypical collagen fibril—has...
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An isoconversional method is proposed to be used for evaluating activation energy of protein denaturation. Applied to DSC data on collagen denaturation, the method yields an activation energy that decreases throughout the process. The Lumry-Eyring model gives an explanation for this decrease and affords estimates for the enthalpy of the reversible step and the activation energy of the irreversible step of denaturation. The reversible unfolding is detectable by multi-frequency temperature-modulat...
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The procedures used in some very recent works for evaluation of the kinetic parameters from non-isothermal data corresponding to thermal and thermo-oxidative degradation of polymers and polymeric materials are critically analysed. It is pointed out that only the use of a set of conversion degree vs. temperature curves recorded at different heating rates can give reliable information on the degradation mechanism and in some suitable cases, can lead to the true kinetic parameters. A general algori...
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