温度对鱼鳞胶原蛋白二级结构的影响

Abstract
References
Related Citation (15)

Download: PDF (1998 KB)
Export: BibTeX | EndNote (RIS)

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.

Key words：PSC;Temperature;FTIR;Raman;CD;Secondary structure

Received: 2006-06-12 Accepted: 2006-10-27

ZTFLH:

Q518.1

Corresponding Authors: LI Chun-mei E-mail: lichmyl@126.com

Cite this article:

ZHONG Zhao-hui,LI Chun-mei,GU Hai-feng, et al. Effect of Temperature on the Secondary Structure of Fish Scale Collagen[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(10): 1970-1976.

URL:

https://www.gpxygpfx.com/EN/Y2007/V27/I10/1970

[1] Nomura Y, Sakai H, Ishii Y, et al. Bioscience, Biotechnology and Biochemistry, 1996, 60: 2092.
[2] Ogawa M, Portier R J, Moody M W, et al. Food Chemistry, 2004, 88(4): 495.
[3] Ikoma T, Kobayashi H, Tanaka J, et al., International Journal of Biological Macromolecules, 2003, 32(3-5): 199.
[4] Nagai T, Izumi M, Ishii M. International Journal of Food Science and Technology, 2004, 39: 239.
[5] Kimura S, Zhu X, Matsui R, et al. Journal of Food Science, 1988, 23: 1315.
[6] DONG Rui-xin, YAN Xun-ling, JIANG Shan(董瑞新, 闫循领, 江山). Spectroscopy and Spectral Analysis(光谱学与光谱分析), 2004, 24(11): 1367.
[7] XIAO He-lan, SUN Su-qin, ZHOU Qun(肖和兰, 孙素琴, 周群). J. of Atom. and Molec. Phys.(原子与分子物理学报), 2003, 20(2): 211.
[8] LIU Qing-hui, WANG Cai-li, LIU Cong-li(刘庆慧, 王彩理, 刘丛力). Marine Fisheries Research(海洋水产研究), 2000, 21(3): 57.
[9] WANG Jia-zheng, FAN Ming(汪家政, 范明). The Handbook of Protein Technology(蛋白质技术手册). Beijing：Science Press(北京：科学出版社)，2000.
[10] Saito M, Takenouchi Y, Kunisaki Y, et al. European Journal of Biochemistry, 2001, 268: 2817.
[11] Yoshida C, Fujisawa S, Mizuta S, et al. Journal of Food Science, 2001, 66: 247.
[12] Nagai T, Suzuki N. Food Chemistry, 2000, 68: 277.
[13] Senaratne L S, Park P J, Kim S K. Bioresource Technololy, 2006, 97: 191.
[14] Sivakumar P, Arichandran A, Suguna L, et al. Journal of Fish Biology, 2000, 56: 999.
[15] Doyle B B. Biopolymers, 1975, 14(5): 937.
[16] Chang Myung Chul, Tanaka Junzo. Biomaterials, 2002, 23: 4811.
[17] Jackson M, Lin-P'ing Choo, Watson P H, et al. Biochimica et Biophysica Acta, 1995, 1270(1): 1.
[18] Li He, Chen Hua Lin, Luo Rong. Macromol. Bioscience, 2003, 3(7): 344.
[19] Usha R, Ramasami T. Colloids and Surfaces B: Biointerfaces，2005，41：21.
[20] ZHANG Shu-liang, YI Da-nian, WU Tian-ming(张叔良, 易大年, 吴天明). The New Technology and FTIR Spectra Analysis(红外光谱分析与新技术). Beijing: Science and Technology Press of Chinese Medicine(北京: 中国医药科技出版社), 1993. 243.