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| The Effect of Hydroxylation on the Thermal Stability of Rat Collagen |
| JIAO Yun1,2, KONG Ying-jun2, GAO Jian-ping2, KANG Ji-yao2, SUN Kun1,2, ZHA Sheng-hua2, ZHANG Gui-feng2, WANG Ming-lin1 |
1. College of Food Science, Shandong Agricultural University, Taian 271000, China;
2. Institute of Process Engineering, Chinese Academy of Sciences, National Key Laboratory of Biochemical Engineering, Beijing 100190, China |
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Abstract The effect of proline hydroxylation on the thermal stability of collagen was investigated. Skin collagen from BN rats with different weeks were separated and purified. The hydroxyproline (Hyp) content in these collagen were analyzed. The influence of hydroxyproline content on the denaturation process of collagen were investigated using the differential scanning calorimeter (DSC) and the circular dichroism (CD) spectroscopy. The CD spectra indicated that collagen obtained from rat skin had the secondary structure typical for collagen. The helix content decreased when denatured by heat treatment. The denaturation temperature and molar enthalpy change was determined using DSC. The results show that the triple-helix become disordered at 41.3℃(Tm). The molar enthalpy change increased with quantity of hydroxylation of proline. CD spectrum manifested that part of the triple-helix changed into random coil structure when the denaturation temperature was higher than 41.3℃. The result indicates that the hydroxylation of proline modification is the key factor affecting on the structure of collagen during denaturation process.
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Received: 23 March 2015
Published: 24 November 2015
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