碱发温度对毛肚胶原蛋白结构的影响

本文采用酸酶复合法提取毛肚胶原蛋白为原料，利用紫外分光光度计、荧光分光光度计、红外光谱仪和扫描电镜等，分析NaOH涨发温度（40~60 ℃）对毛肚胶原蛋白结构的影响。结果表明，NaOH涨发会导致毛肚胶原蛋白紫外吸收强度减小；随着涨发温度升高，毛肚胶原蛋白荧光强度逐渐降低，巯基含量逐渐增加，导致胶原蛋白变性程度逐渐加深最终完全变性；当涨发温度高于60 ℃，毛肚胶原蛋白表面疏水性呈现下降趋势。随着涨发温度的升高，毛肚胶原蛋白微观结构表现为胶原分子收缩，逐渐卷曲，加快凝集，缝隙减小，片状胶原破碎。因此，NaOH涨发会破坏毛肚胶原蛋白二级结构，表现为断裂、破碎、拉伸、疏松，且不同涨发温度对胶原蛋白结构具有显著影响。

Effect of Temperatures during the Lye Macerating on the Structure of Tripe Collagen

In this paper, acidase compound method was used to extract collagen from tripe. The effects of NaOH rising temperature (40~60 ℃) on collagen structure of tritrium hairy were analyzed by UV spectrophotometer, fluorescence spectrophotometer, infrared spectrometer and scanning electron microscope. The results showed that the the lye macerating of tripe could decrease the UV absorption intensity of collagen in tribolus. With the increase of temperature during the lye macerating of tripe, the fluorescence intensity of collagen decreased and the content of sulfhydryl group increased. It indicated that heating treatment will gradually deepen the degeneration degree of collagen and eventually complete degeneration. When the temperature was 60 ℃, the surface hydrophobicity of tribolus collagen decreased. With the increase of temperature during the lye macerating of tripe, the microstructure of collagen of tripe showed that collagen molecules shrunk, gradually curled, accelerate agglutination, gap decrease and flake collagen was broken. Therefore, NaOH can destroy the secondary structure of collagen in tripe, presenting as fracture, fragmentation, stretching and loosening, and different temperature of hyperplasia has a significant impact on the structure of collagen.