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. 2016 Feb 29;25(1):131–136. doi: 10.1007/s10068-016-0020-z

Comparison of collagen characteristics of sea- and freshwater-rainbow trout skin

Jun Kyu Lee 1, Sang In Kang 1, Yong Jung Kim 1, Min Joo Kim 1, Min Soo Heu 2, Byeong Dae Choi 1, Jin-Soo Kim 1,
PMCID: PMC6049368  PMID: 30263248

Abstract

Proximate composition, volatile basic nitrogen content, and concentrations of collagen in skin samples from either sea- (S-RT) or freshwater-rainbow trout (F-RT) were characterized and compared, to assess the effect of the sea or freshwater habitat on these parameters. Results of amino acid composition, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, thermal denaturation assay and Fourier transform infrared (FT-IR) spectroscopy of acid-soluble collagens were comparable between the two sample sets. Both acid-soluble collagens from sea- and freshwater-rainbow trout skins contained glycine as the major amino acid and high alanine, proline, and hydroxyproline contents, and was found to be predominantly composed of α1-, α2-, and β-chains. FT-IR spectra of ASCs from S-RT and F-RT skins were quite similar. These findings suggest that different rainbow trout habitats (seawater and freshwater) do not affect amino acid composition and molecular weight properties of ASCs from S-RT and F-RT skins.

Keywords: sea-rainbow trout, trout, fish skin collagen, acid-soluble collagen, Oncorhynchus mykiss

References

  • 1.Heu MS, Kim HJ, Ham JS, Park SH, Kim HS, Kang KT, Jee SJ, Lee JH, Kim JS. Preparation and quality characteristics of seasoned and dried fish slice products using rainbow trout (Onchorhynchus mykiss) J. Korean Soc. Food Sci. Nutr. 2008;37:348–356. doi: 10.3746/jkfn.2008.37.3.348. [DOI] [Google Scholar]
  • 2.Kim PK, Jeon JK, Huh HT, Jo JY. Effects of dietary soybean meal in rainbow trout (Oncorhynchus mykiss). II. On the apparent digestibility, excretion and body composition. J. Aquacultur. 1996;9:395–407. [Google Scholar]
  • 3.Ermana DC, Hawthorneb VM. The quantitative importance of an intermittent stream in the spawning of rainbow trout. T. Am. Fish. Soc. 1976;105:675–681. doi: 10.1577/1548-8659(1976)105<675:TQIOAI>2.0.CO;2. [DOI] [Google Scholar]
  • 4.Kim KH, Kang SI, Jeon YJ, Choi BD, Kim MW, Kim DS, Kim JS. Food quality of rainbow trout Oncorhynchus mykiss domesticated in seawater. Korean J. Fish. Aquat. Sci. 2014;47:114–121. doi: 10.5657/KFAS.2014.0114. [DOI] [Google Scholar]
  • 5.Chang YJ, Hur JW, Lim HK, Lee JK. Stress in olive flounder (Paralichthys olivaceus) and fat cod (Hexagrammos otakii) by the sudden drop and rise of water temperature. Korean^J. Fish. Aquat. Sci. 2001;34:91–97. [Google Scholar]
  • 6.Kaewdang O, Benjakul S, Kaewmanee T, Kishimura H. Characteristics of collagens from the swim bladders of yellowfin tuna (Thunnus albacares) Food Chem. 2014;155:264–270. doi: 10.1016/j.foodchem.2014.01.076. [DOI] [PubMed] [Google Scholar]
  • 7.Nikoo M, Benjakul S, Bashari M, Alekhorshied M, Cissouma AI, Yang N, Xu X. Physicochemical properties of skin gelatin from farmed Amur sturgeon (Acipenser schrenckii) as influenced by acid pretreatment. Food Bioscienc. 2014;5:19–26. doi: 10.1016/j.fbio.2013.10.004. [DOI] [Google Scholar]
  • 8.Singh P, Benjakul S, Maqsood S, Kishimura H. Isolation and characterization of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus) Food Chem. 2011;124:97–105. doi: 10.1016/j.foodchem.2010.05.111. [DOI] [Google Scholar]
  • 9.Jeevithan E, Wu W, Nanping W, Lan H, Bao B. Isolation, purification and characterization of pepsin soluble collagen isolated from silvertip shark (Carcharhinus albimarginatus) skeletal and head bone. Process Biochem. 2014;49:1767–1777. doi: 10.1016/j.procbio.2014.06.011. [DOI] [Google Scholar]
  • 10.Kim JS, Park JW. Characterization of acid-soluble collagen from Pacific whiting surimi processing byproducts. J. Food Sci. 2004;69:C637–C642. doi: 10.1111/j.1365-2621.2004.tb09912.x. [DOI] [Google Scholar]
  • 11.Ogawa M, Moody MW, Portier RJ, Bell J, Schexnayder MA, Losso JN. Biochemical properties of black drum and sheephead seabream skin collagen. J. Agr. Food Chem. 2003;11:8088–8092. doi: 10.1021/jf034350r. [DOI] [PubMed] [Google Scholar]
  • 12.Park CH, Lee JH, Kang KT, Park JW, Kim JS. Characterization of acid-soluble collagen from Alaska pollock surimi processing by-products (refiner discharge) Food Sci. Biotechnol. 2007;16:549–556. [Google Scholar]
  • 13.Siddiqui YD, Arief EM, Yusoff A, Hamid SSA, Norani TY, Abdullah MYS. Extraction purification and physical characterization of collagen from body wall of sea cucumber Bohadschia bivitatta. Health Environ. J. 2013;4:53–65. [Google Scholar]
  • 14.AOAC. Official Methods of Analysis. 2000. [Google Scholar]
  • 15.Bligh EG, Dyer WJ. A rapid method of lipid extraction and purification. Can. J. Biochem. Phys. 1959;37:911–917. doi: 10.1139/o59-099. [DOI] [PubMed] [Google Scholar]
  • 16.Kapute F, Likonwe J, Kangombe J. Quality assessment of fresh lake Malawi tilapia (Chambo) collected from selected local and super markets in Malawi. Internet^J. Food Safet. 2012;14:113–121. [Google Scholar]
  • 17.Kimura S, Zhu XP, Matsui R, Shijoh M, Takamizawa S. Characterization of fish muscle type I collagen. J. Food Sci. 1988;53:1315–1318. doi: 10.1111/j.1365-2621.1988.tb09266.x. [DOI] [Google Scholar]
  • 18.Laemmli VK. Cleavage of structural proteins during the assembly of the heads of bacteriophage T4. Natur. 1970;227:680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  • 19.Zhu XP, Kimura S. Thermal stability and subunit composition of muscle and skin type I collagens from skipjack. Nippon Suisan Gakk. 1991;57:755–760. doi: 10.2331/suisan.57.755. [DOI] [Google Scholar]
  • 20.Kim HJ, Jee SJ, Yoon MS, Yoon MH, Kang KT, Lee DH, Heu MS, Kim JS. Characterization of acid-and pepsin-soluble collagens from rockfish Sebastes schlegeli skin. J. Fish. Sci. Technol. 2009;12:6–15. [Google Scholar]
  • 21.Muyonga JH, Cole CGB, Duodu KG. Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus) Food Chem. 2004;86:325–332. doi: 10.1016/j.foodchem.2003.09.038. [DOI] [Google Scholar]
  • 22.Kim JS, Kim IS, Heu MS, Kong CS, Lee TG, Yeum DM, Kang HG. The principle and application of canned food. 2002. pp. 205–212. [Google Scholar]
  • 23.Montero P, Borderias J, Turnay J, Leyzarbe MA. Characterization of hake (Merluccius merluccius L.) and trout (Salmo irideus Gibb) collagen. J. Agr. Food Chem. 1990;38:604–609. doi: 10.1021/jf00093a004. [DOI] [Google Scholar]
  • 24.Kimura S, Ohno Y. Fish type I collagen tissue specific existence of 2 molecular forms, (α1)2α2 and α1α2α3, in Alaska pollock. Comp. Biochem. Physiol. 1987;88b:409–413. [Google Scholar]
  • 25.Hamada H. Effects of the preparation conditions on the physical properties of shark-skin gelatin gels. Nippon Suisan Gakk. 1990;56:671–677. doi: 10.2331/suisan.56.671. [DOI] [Google Scholar]
  • 26.Yata M, Yoshida C, Fujisawa S, Mizuta S, Yoshinaka R. Identification and characterization of molecular species of collagen in fish skin. J. Food Sci. 2001;66:247–251. doi: 10.1111/j.1365-2621.2001.tb11325.x. [DOI] [Google Scholar]
  • 27.Norland RE. Fish gelatin. In: Voigt MN, Botta JR, editors. Advances in Fisheries Technology and Biotechnology for Increased Profitability. 1990. pp. 325–333. [Google Scholar]
  • 28.Petibois C, Deleris G. Chemical mapping of tumor progression by FT-IR imaging: Towards molecular histopathology. Trends Biotechnol. 2006;24:455–462. doi: 10.1016/j.tibtech.2006.08.005. [DOI] [PubMed] [Google Scholar]
  • 29.Doyle BB, Bendit EG, Blout ER. Infrared spectroscopy of collagen and collagenlike polypeptides. Biopolymer. 1975;14:937–957. doi: 10.1002/bip.1975.360140505. [DOI] [PubMed] [Google Scholar]
  • 30.Wang L, Liang Q, Chen T, Wang Z, Xu J, Ma H. Characterization of collagen from the skin of Amur srurgen (Acipenser schrenckii) Food Hydrocolloid. 2014;38:104–109. doi: 10.1016/j.foodhyd.2013.12.002. [DOI] [Google Scholar]
  • 31.Liu D, Zhou P, Li T, Regenstein JM. Comparison of acid-soluble collagens from the skins and scales of four carp species. Food Hydrocolloid. 2014;41:290–297. doi: 10.1016/j.foodhyd.2014.04.030. [DOI] [Google Scholar]
  • 32.Pati F, Adhikari B, Dhara S. Isolation and characterization of fish scale collagen of higher thermal stability. Bioresource Technol. 2010;101:3737–3742. doi: 10.1016/j.biortech.2009.12.133. [DOI] [PubMed] [Google Scholar]
  • 33.Muyonga JH, Cole CGB, Doudu KG. Characterisation of acid soluble collagen from skins of young and adult Nile perch (Lates niloricus) Food Chem. 2004;85:81–89. doi: 10.1016/j.foodchem.2003.06.006. [DOI] [Google Scholar]
  • 34.Woo JW, Yu SJ, Cho SM, Lee YB, Kim SB. Extraction optimization and properties of collagen from yellowfin tuna (Thunnus albacares) dorsal skin. Food Hydrocolloid. 2008;22:879–887. doi: 10.1016/j.foodhyd.2007.04.015. [DOI] [Google Scholar]

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