Study On The Effect Of Hydroxylation Modification On Thermal Stability Of Rat Collagen
Keywords
Collagen, Circular Dichroism Spectroscopy, Hydroxylation Modification, Thermal Stability, Differential Scanning Calorimeter
Abstract
Differential scanning calorimetry (DSC) was used to study the effect of hydroxyproline (Hyp) content on the thermal stability of collagen. Collagen was prepared from the skin of BN rats of different ages as raw material, and the Hyp content in the prepared collagen was analyzed; DSC was used to determine the critical denaturation temperature and enthalpy change of collagen with different Hyp contents; circular dichroism (CD) was used to detect the dichromatism of the extracted collagen. level structure. The results show that the extracted collagen undergoes triple helix depolymerization at 41.3¡ãC. CD spectrum analysis results show that when the sample is treated at the critical denaturation temperature, part of the triple helix structure is transformed into a random coil structure. The heat required during collagen denaturation is positively correlated with the hydroxyproline content. The experiment established the relationship between the enthalpy change and Hyp content during the thermal denaturation of collagen. This study shows that proline hydroxylation modification in collagen is a key factor affecting the thermal stability of collagen.
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Original research was done by Kong Yingjun, Sun Kun, Kang Jiyao, Zhang Guifeng, Zha Shenghua, Jiao Yun, Wang Minglin, Gao Jianping
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