Abstract:Pepsin-soluble collagen (PSC) was extracted from fish scale of grass carp and was analyzed by SDS-PAGE, which confirmed that PSC are typical type Ⅰcollagen and reach electrophoretic purity. Effect of temperature on the secondary structure of collagen was studied by FTIR, Raman and CD. FTIR indicated that the fish scale PSC had typically characteristic absorptions of collagen, and 1659, 1552 and 1238cm-1 were assigned to be amide Ⅰ, Ⅱ and Ⅲ respectively. When the temperature increased, amide A and amide B shifted to low frequency, the absorption of 1658cm-1 split into several absorption peaks, the absorption at 1552cm-1 had a slight red-shift followed by a distinct blue-shift, and the frequency of 1238cm-1 declined. Raman spectra showed that the absorptions of amideⅠ, amideⅡ and amide Ⅲ appeared at 1669, 1557 and 1245cm-1 respectively, which were higher than those in FTIR spectra. Furthermore, the characteristic absorptions of proline at 921 and 855cm-1 only appeared in Raman spectra. CD spectra demonstrated a rotatory maximum at 221.6nm and a negative peak at 204.4nm of PSC solution, which were typical spectral characteristics of the collagen triple helix structure. The structure changes of the lyophilized PSC appeared mainly between 35 and 60℃ in FTIR and Raman spectra, yet CD spectra demonstrated that the configurational changes of PSC in acidic solution appeared in the range of 20 to 35℃, indicating that the lyophilized PSC was more stable than the acidic solution of PSC.
钟朝辉,李春美*,顾海峰,窦宏亮,周丽明. 温度对鱼鳞胶原蛋白二级结构的影响[J]. 光谱学与光谱分析, 2007, 27(10): 1970-1976.
ZHONG Zhao-hui, LI Chun-mei*, GU Hai-feng, DOU Hong-liang, ZHOU Li-ming. Effect of Temperature on the Secondary Structure of Fish Scale Collagen. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(10): 1970-1976.
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