Characterization of Acid-Soluble Collagen from Skins of Surf Smelt (Hypomesus pretiosus japonicus Brevoort)

Takeshi Nagai

.

DOI: 10.4236/fns.2010.12010                

Abstract

Acid-soluble collagen was extracted from the skins of surf smelt and characterized. The yield of collagen was high about 24.0% on a dry weight basis. By SDS-polyacrylamide gel electrophoresis and CM-Toyopearl 650 M column chromatography, this collagen is a heterotrimer with a chain composition of α1α2α3. The denaturation temperature was 32.5℃, about 4.5℃ lower than that from porcine skin. Attenuated total reflectance-fourier transform infrared analysis showed that the percentage of secondary structural components in this collagen were 11% α-helix, 34% β-sheet, 19% β-turn, and 21% others. It suggests that the triple helical structure is present in the acid-soluble collagen from the skins of the surf smelt in comparison to that from the skin of porcine.

Keywords

Attenuated Total Reflectance-Fourier Transform Infrared (ATR-FTIR) Analysis, Collagen, Denaturation Temperature, Skin, Surf Smelt

Conflicts of Interest

The authors declare no conflicts of interest.

References

[1]	A. Jongjareonrak, S. Benjakul, W. Visessanguan, T. Nagai and M. Tanaka, “Isolation and Characterization 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.
[2]	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.
[3]	T. Nagai, “Collagen from Diamondback Squid (Thysanoteuthis rhombus) Outer Skin,” Zeitschrift für Naturforschung, Vol. 59, No. 3-4, 2004, pp. 271-275.
[4]	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.
[5]	T. Nagai, W. Worawattanamateekul, 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.
[6]	T. Nagai, E. Yamashita, K. Taniguchi, N. Kanamori and N. Suzuki, “Isolation and Characterization of Collagen from the Outer Skin Waste Material of Cuttlefish (Sepia lycidas),” Food Chemistry, Vol. 72, No. 4, 2001, pp. 425-429.
[7]	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.
[8]	T. Nagai, K. Nagamori, R. 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.
[9]	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.
[10]	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.
[11]	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.
[12]	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.
[13]	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.
[14]	T. Nagai, N. Suzuki and T. Nagashima, “Collagen from Common Minke Whale (Balaenoptera acutorostrata) Unesu,” Food Chemistry, Vol. 111, No. 2, 2008, pp. 296-301.
[15]	E. Chung and E. J. Miller, “Collagen Polymorphism: Characterization of Molecules with the Chain Composition [α1(III)]3 in Human Tissues,” Science, Vol. 183, No. 4130, 1974, pp. 1200-1201.
[16]	R. K. Rhodes and E. J. Miller, “Physicochemical Characterization and Molecular Organization of the Collagen A and B Chains,” Biochemistry, Vol. 17, No. 1, 1978, pp. 3442-3448.
[17]	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.
[18]	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-E455.
[19]	Y. Zhang, W. Liu, G. Li, B. Shi, Y. Miao and X. Wu, “Isolation and Partial Characterization of Pepsin-Solu- ble Collagen from the Skin of Grass Carp (Ctenopharyngodon idella),” Food Chemistry, Vol. 103, No. 4, 2007, pp. 906-912.
[20]	S. Kimura, Y. Ohno, Y. Miyauchi and N. Uchida, “Fish Skin Type I Collagen: Wide Distribution of α3 Subunit in Teleosts,” Comparative Biochemistry and Physiology, Vol. 88B, No. 2, 1987, pp. 27-34.
[21]	S. Kimura and Y. Ohno, “Fish type I collagen: Tissue-Specific Existence of Two Molecular Forms, (α1)2α2 and α1α2α3, in Alaska Pollack,” Comparative Biochemistry and Physiology, Vol. 88B, No. 2, 1987, pp. 409-413.
[22]	B. J. Rigby, “Amino-acid Composition and Thermal Stability of the Skin Collagen of the Antarctic Ice- Fish,” Nature, Vol. 219, No. 5150, 1968, pp. 166-167.
[23]	M. Ando, M. Ando, M. Makino, Y. Tsukamasa, Y. Makinodan and M. Miyoshi, “Interdependence between Heat Solubility and Pyridinoline Contents of Squid Mantle Collagen,” Journal of Food Science, Vol. 66, No. 2, 2001, pp. 265-269.
[24]	P. Kittiphattanabawon, S. Benjakul, W. Visessanguan, T. Nagai and N. 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.
[25]	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.
[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.
[27]	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.
[28]	W. K. Surewicz and H. H. Mantsch, “New Insight into Protein Secondary Structure from Resolution Enhanced Infrared Spectra,” Biochimica et Biophysica Acta, Vol. 952, No. 2, 1988, pp. 115-130.
[29]	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. 89-100.