Collagen from Tendon of Yezo Sika Deer (Cervus nippon yesoensis) as By-Product
Takeshi Nagai, Nobutaka Suzuki, Yasuhiro Tanoue, Norihisa Kai
DOI: 10.4236/fns.2012.31012   PDF   HTML     5,625 Downloads   9,215 Views   Citations


Collagen from tendon of Yezo sika deer was prepared by limited pepsin digestion. The yield of collagen was very high; 35.7% on the basis of lyophilized dry weight. The secondary structure of this collagen was different from that of porcine skin by ATR-FTIR analysis, although it was the same characteristics, e.g. SDS-PAGE, subunit composition, ther-mal behavior, as porcine collagen. Since taking up a problem of bovine spongiform encephalopathy infection in land animals such as calf or bovine, collagen from aquatic materials has been used in various industries. However, the present study indicates that tendon of Yezo sika deer as by-product of meat industry will have potential as an important collagen source for use in the foods, cosmetics, and medical fields.

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T. Nagai, N. Suzuki, Y. Tanoue and N. Kai, "Collagen from Tendon of Yezo Sika Deer (Cervus nippon yesoensis) as By-Product," Food and Nutrition Sciences, Vol. 3 No. 1, 2012, pp. 72-79. doi: 10.4236/fns.2012.31012.

Conflicts of Interest

The authors declare no conflicts of interest.


[1] A. Jongjareonrak, S. Benjakul, W. Visessanguan, T. Nagai and M. Tanaka, “Isolation and Characterisation of Acid and Pepsin-Solubilised Collagens from the Skin of Brownstripe Red Snapper (Lutjanus vitta),” Food Chemistry, Vol. 93, No. 3, 2005, pp. 475-484. doi:10.1016/j.foodchem.2004.10.026
[2] 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 Agriculture, Vol. 79, No. 6, 1999, pp. 855-858. doi:10.1002/(SICI)1097-0010(19990501)79:6<855::AID-JSFA299>3.0.CO;2-N
[3] T. Nagai, W. Worawattabamateekul, N. Suzuki, T. Nakamura, T. Ito, K. Fujiki, M. Nakao and T. Yano, “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
[4] T. Nagai, E. Yamashita, K. Taniguchi, N. Kanamori and N. Suzuki, “Isolation and Characterisation of Collagen from the Outer Skin Waste Material of Cuttlefish (Sepia lycidas),” Food Chemistry, Vol. 72, No. 4, 2001, pp. 425-429. doi:10.1016/S0308-8146(00)00249-1
[5] 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. 173-177. doi:10.1016/S0308-8146(01)00396-X
[6] T. Nagai, K. Nagamori, E. Yamashita and N. Suzuki, “Collagen of Octopus Callistoctopus arakawai Arm,” International Journal of Food Science and Technology, Vol. 37, No. 3, 2002, pp. 285-289.
[7] T. Nagai, M. Izumi and M. Ishii, “Fish Scale Collagen. Preparation and Partial Characterization,” International Journal of Food Science and Technology, Vol. 39, No. 3, 2004, pp. 239-244. doi:10.1111/j.1365-2621.2004.00777.x
[8] 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
[9] T. Nagai and N. Suzuki, “Partial Characterization of Collagen from Purple Sea Urchin (Anthocidaris crassispina) Test,” International Journal of Food Science and Technology, Vol. 35, No. 5, 2000, pp. 497-501. doi:10.1046/j.1365-2621.2000.00406.x
[10] T. Nagai and N. Suzuki, “Preparation and Characterization of Several Fish Bone Collagens,” Journal of Food Biochemistry, Vol. 24, No. 5, 2000, pp. 427-436. doi:10.1111/j.1745-4514.2000.tb00711.x
[11] T. Nagai and N. Suzuki, “Preparation and Partial Characterization of Collagen from Paper Nautilus (Argonauta argo, Linnaeus) Outer Skin,” Food Chemistry, Vol. 76, No. 2, 2002, pp. 149-153. doi:10.1016/S0308-8146(01)00255-2
[12] T. Nagai, N. Suzuki and T. Nagashima, “Collagen from Common Minke Whale (Balaenoptera acutorostrata) Une- su,” Food Cshemistry, Vol. 111, No. 2, 2008, pp. 296-301. doi:10.1016/j.foodchem.2008.03.087
[13] U. K. Laemmli, “Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4,” Nature, Vol. 227, 1970, pp. 680-685. doi:10.1038/227680a0
[14] T. Nagai, “Collagen from Diamondback Squid (Thysanoteuthis rhombus) Outer Skin,” Zeitschrift für Naturforschung, Vol. 59c, 2004, pp. 271-275.
[15] 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
[16] L. Wang, X. An, Z. Xin, L. Zhao 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. E450-455. doi:10.1111/j.1750-3841.2007.00478.x
[17] Y. Zhang, W. Liu, G. Li, B. Shi, Y. Miao and X. Wu, “Isolation and Partial Characterization of Pepsin-Soluble Collagen from the Skin of Grass Carp (Ctenopharyngodon idella),” Food Chemistry, Vol. 103, No. 3, 2007, pp. 906-912. doi:10.1016/j.foodchem.2006.09.053
[18] S. Cliche, J. Amiot, C. Avezard and C. Gariépy, “Extraction and Characterization of Collagen with or without Telopeptides from Chicken Skin,” Poultry Science, Vol. 82, No. 3, 2003, pp. 503-509.
[19] T. Nagai, “Characterization of Collagen from Japanese Sea Bass Caudal Fin as Waste Material,” European Food Research and Technology, Vol. 218, No. 5, 2004, pp. 424-427. doi:10.1007/s00217-004-0892-7
[20] B. J. Rigby, “Amino-Acid Composition and Thermal Stability of the Skin Collagen of the Antarctic Ice-fish,” Nature, Vol. 219, 1968, pp. 166-167. doi:10.1038/219166a0
[21] P. Kittiphattanabawon, S. Benjakul, W. Visessanguan, T. Nagai and M. Tanaka, “Characterisation of Acid-Soluble Collagen from Skin and Bone of Bigeye Snapper (Priacanthus tayenus),” Food Chemistry, Vol. 89, No. 3, 2005, pp. 363-372. doi:10.1016/j.foodchem.2004.02.042
[22] M. Yan, B. Li, X. Zhao, G. Ren, Y. Zhuang, H. Hou, X. Zhang, Li. Chen and Y. Fan, “Characterization of Acid-Soluble Collagen from the Skin of Walleye Pollack (Theragra chalcogramma),” Food Chemistry, Vol. 107, No. 4, 2008, pp. 1581-1586. doi:10.1016/j.foodchem.2007.10.027
[23] J. H. Muyonga, C. G. B. Cole and K. G. Duodu, “Characterisation of Acid Soluble Collagen from Skins of Young and Adult Nile Perch (Lates niloticus),” Food Chemistry, Vol. 85, No. 1, 2004, pp. 81-89. doi:10.1016/j.foodchem.2003.06.006
[24] K. J. Payne and A. Veis, “Fourier Transform IR Spectroscopy of Collagen and Gelatin Solutions: Deconvolution of the Amide I Band for Conformational Studies,” Biopolymers, Vol. 27, No. 11, 1988, pp. 1749-1760. doi:10.1002/bip.360271105
[25] W. K. Surewicz and H. H. Mantsch, “New Insight into Protein Secondary Structure from Resolution Enhanced Infrared Spectra,” Biochimica Biophysica Acta, Vol. 952, 1988, pp. 115-130. doi:10.1016/0167-4838(88)90107-0
[26] B. B. Doyle, E. G. Bendit and E. R. Blout, “Infrared Spectroscopy of Collagen and Collagen-like Polypeptides,” Biopolymers, Vol. 14, No. 5, 1975, pp. 937-957. doi:10.1002/bip.1975.360140505
[27] R. W. Sarver Jr. and W. C. Krueger, “Protein Secondary Structure from Fourier Transform Infrared Spectroscopy: A Data Base Analysis,” Analytical Biochemistry, Vol.194, No. 1, 1991, pp. 39-100.

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