Preparation and Characterisation of Collagen from Freshwater Fish Scales

DOI: 10.4236/fns.2011.28112   PDF   HTML     12,126 Downloads   25,201 Views   Citations


Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2. Compared with the carp fish ordinary muscle type I collagen , porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spacings (d) of about 4.48 Å and 11.87 Å. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.

Share and Cite:

F. Zhang, A. Wang, Z. Li, S. He and L. Shao, "Preparation and Characterisation of Collagen from Freshwater Fish Scales," Food and Nutrition Sciences, Vol. 2 No. 8, 2011, pp. 818-823. doi: 10.4236/fns.2011.28112.

Conflicts of Interest

The authors declare no conflicts of interest.


[1] H. Onozato and N. Watabe, “Studies on Fish Scale Formation and Resorption,” Cell and Tissue Research, Vol 201, No. 3, 1980, pp. 303-316. doi:10.1007/BF00236999
[2] L. Zylberberg, J. Bereiter-Hahn and J.-Y. Sire, “Cytoskeletal Organization and Collagen Orientation in the Fish Scales,” Cell and Tissue Research, Vol. 253, No. 3, 1988, pp. 597-607. doi:10.1007/BF00219750
[3] T. Ikoma, H. Kobayashi, J. Tanaka, D. Walsh and S. Mann, “Microstructure, Mechanical, and Biomimetic Properties of Fishscales from Pagrus Major,” Journal of Structural Biology, Vol. 142, No. 3, 2003, pp. 327-333. doi:10.1016/S1047-8477(03)00053-4
[4] M. Ogawa, R. J. Portier, M. W. Moody, J. Bell, M. A.Schexnayder and J. N. Losso, “Biochemical Properties of Bone and Scale Collagens Isolated from the Subtropical Fish Black Drum (Pogonia Cromis) and Sheepshead Seabream (Archosargus Probatocephalus),” Food Chemistry, Vol. 88, No. 4, 2004, pp. 495-501. doi:10.1016/j.foodchem.2004.02.006
[5] T. Ikoma, H. Kobayashi, J. Tanaka, D. Walsh and S. Mann, “Physical Properties of Type I Collagen Extracted from Fish Scales of Pagrus Major and Oreochromis Niloticas,” International Journal of Biological Macromolecules, Vol. 32, No. 3-5, 2003, pp. 199-204. doi:10.1016/S0141-8130(03)00054-0
[6] T. Nagai, W. Worawattanamateekul, N. Suzuki, T. Nakamura, T. Ito, et al., “Isolation and Characterization of Collagen from Rhizostomous Jellyfish (Rhopilema Asamushi),” Food Chemistry, Vol. 70, No. 2, 2000, pp. 205-208. doi:10.1016/S0308-8146(00)00081-9
[7] U. K. Laemmli, “Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4,” Nature, Vol. 227, No. 5259, 1970, pp. 680-685. doi:10.1038/227680a0
[8] T. Nagai, T. Ogawa, T. Nakamura, T. Ito, H. Nakagawa, K. Fujiki, M. Nakao and T. Yano, “Collagen of Edible Jellyfish Exumbrella,” Journal of the Science of Food and Agriculture, Vol. 79, No. 6,1999, pp. 855-858. doi:10.1002/(SICI)1097-0010(19990501)
[9] O. P. Oslon and N. Watabe, “Studies on Formation and Resorption of Fish Scales,” Cell and Tissue Research, Vol. 211, No. 2, 1980, pp. 303-316. doi:10.1007/BF00236451
[10] S. Kimura, Y. Ohno, Y. Miyauchi and N. Uchida, “Fish Skin Type I Collagen: Wide Distribution of an a3 Subunit in Teleosts,” Comparative Biochemistry and Physiology, Vol. 88B, No. 1, 1987, pp. 27-34. doi:10.1016/0305-0491(92)90119-C
[11] S. Kimura, “Wide Distribution of the Skin Type I Collagen α3 Chain in Bony Fish,” Comparative Biochemistry and Physiology, Vol. 102B, No. 2, 1992, pp. 255-260. doi:10.1016/0305-0491(92)90119-C
[12] K. Sato, R. Yoshinaka, M. Sato, Y. Itoh and Y. Shimizu, “Isolation of Types I and V Collagens from Carp Muscle,” Comparative Biochemistry and Physiology, Vol. 90B, No. 1, 1988, pp. 155-158. doi:10.1016/0305-0491(88)90053-3
[13] M. Nishimoto, R. Sakamoto, S. Mizuta and R. Yoshinaka, “Identification and Characterization of Molecular Species of Collagen in Ordinary Muscle and Skin of the Japanese flounder Paralichthys Olivaceus,” Food Chemistry, Vol. 90, No. 1-2, 2005, pp. 151-156. doi:10.1016/j.foodchem.2004.03.034
[14] J.-H. wang, S. Mizuta, Y. Yokoyama and R. Yoshinaka, “Purification and Characterization of Molecular Species of Collagen in the Skin of Skate (Raja kenojei),” Food Chemistry, Vol. 100, No. 3, 2007, pp. 921-925. doi:10.1016/j.foodchem.2005.10.046
[15] M. S. Heu, J. H. Lee, H. J. Kim, S. J. Jee, J. S. Lee, Y. J. Jeon, F. Shahidi and J.-S. Kim, “Characterization of Acid- and Pepsin-Soluble Collagens from Flatfish Skin,” Food Science Biotechnology, Vol. 19, No. 1, 2010, pp. 27-33. doi:10.1007/s10068-010-0004-3
[16] L. Wang, X. An, Z. Xin, L. Zaho and Q. Hu, “Isolation and Characterization of Collagen from the Skin of Deep-Sea Redfish (Sebastes Mentella),” Journal of Food Science, Vol. 72, No. 8, 2007, pp. E450-E455. doi:10.1111/j.1750-3841.2007.00478.x
[17] T. Nagai and N. Suzuki, “Isolation of Collagen from Fish Waste Material—Skin, Bone and Fins,” Food Chemistry, Vol. 68, No. 3, 2000, pp. 277-281. doi:10.1016/S0308-8146(99)00188-0
[18] T. Nagai, Y. Araki and N. Suzuki, “Collagen of the Skin of Ocellate Puffer Fish (Takifugu Rubripes),” Food Chemistry, Vol. 78, No. 2, 2002, pp. 137-177. doi:10.1016/S0308-8146(01)00396-X
[19] B. J. Rigby, “Amino-Acid Composition and Thermal Stability of the Skin Collagen of the Antarctic Ice-Fish,” Nature, Vol. 219, No. 1, 1968, pp. 166-167. doi:10.1038/219166a0
[20] H. Y. Liu, D. Li and S. D. Guo, “Studies on Collagen from the Skin of Channel Catfish (Ictalurus Punctaus),” Food Chemistry, Vol. 101, No. 2, 2007, pp. 621-625. doi:10.1016/j.foodchem.2006.01.059
[21] A. Bigi, M. Burghammer, R. Falconi, M. H. Koch, S. Panzavolta and C. Riekel, “Twisted Plywood Pattern of Collagen Fibrils in Teleost Scales: An X-ray Diffraction Investigation,” Journal of Structural Biology, Vol. 136, No. 2, 2001, pp. 137-143. doi:10.1006/jsbi.2001.4426
[22] G. J. Cameron, D. E. Cairns and T. J. Wess, “The Variability in Type I Collagen Helical Pitch Is Reflected in the D Periodic Fibrillar Structure,” Journal of Molecular Biology, Vol. 372, No. 4, 2007, pp. 1097-1107. doi:10.1016/j.jmb.2007.05.076

comments powered by Disqus

Copyright © 2020 by authors and Scientific Research Publishing Inc.

Creative Commons License

This work and the related PDF file are licensed under a Creative Commons Attribution 4.0 International License.