Physicochemical Properties and Biological Activities of Collagens with Different Molecular Weights from Alaska Pollack (Theragra chalcogramma) Skin

명태 껍질 유래 콜라겐의 분자량에 따른 이화학적 특성 및 생리활성

  • Yang, Su-Jin (Department of Food Science and Technology, Catholic University of Daegu) ;
  • Hong, Joo-Heon (Department of Food Science and Technology, Catholic University of Daegu)
  • 양수진 (대구가톨릭대학교 식품공학전공) ;
  • 홍주헌 (대구가톨릭대학교 식품공학전공)
  • Received : 2014.06.02
  • Accepted : 2014.07.24
  • Published : 2014.10.31


This study was conducted to investigate the physicochemical properties and biological activities of collagens with different molecular weights from Alaska pollack (Theragra chalcogramma) skin as well as their efficacies as functional materials. The molecular weights of collagens were between 1~10 kDa (below 1 kDa (AP1), 1~3 kDa (AP2), 3~10 kDa (AP3), and above 10 kDa (AP4). The protein content of AP4 (40.19 g/100 g) was the highest. Collagen contents of AP1, AP2, AP3, and AP4 were 36.43, 32.23, 19.23, and 14.89%, respectively. The free amino acid and essential amino acid contents of AP1 were higher than those of AP2, AP3, and AP4. Fourier transform infrared spectroscopy spectra of collagens with different molecular weights showed wavenumbers representing the regions of amide I, amide II, amide III, and amide A, respectively. The electron-donating ability (29.51%) and SOD-like activity (38.45%) of AP1 were higher than those of AP2, AP3, and AP4. Tyrosinase inhibition activity of AP1 improved with higher treatment concentration. The rate of inhibition of MMP-1 production in HS68 cells exposed to UVB was suppressed by treatment with AP1 (29.78%) and AP2 (26.49%) at 1 mg/mL. Furthermore, there was a strong correlation between DPPH, superoxide dismutase, tyrosinase activity, and MMP-1 inhibition rate of collagens with different molecular weights.


Supported by : 산업통상자원부


  1. Park HY, Yoon HD, Hae J. 2006. Development of industrial utilization technique of starfish collagen. Fishery Science & Technology Last Research Report. Ministry of Oceans and Fisheries, Sejong, Korea. p 94-96
  2. Yoo SJ, Cho SM, Woo JW, Kim SH, Han YN, Ahn JR, Kim SY, Kim TW, Kim SB. 2008. Processing and physicochemical properties of collagen from yellowfin tuna (Thunnus albacares) abdominal skin. J Kor Fish Soc 41: 427-434.
  3. Kim SK, Kang OJ, Kwak DC. 1993. Physicochemical characteristics of filefish and cod skin collagen. J Korean Soc Agric Chem Biotechnol 36: 163-171.
  4. Kwon MC, Syed AQ, Kim HS, Ahn JH, Cho NH, Lee HY. 2008. UV protection and whitening effects of collagen isolated from outer layer of the squid Todarodes pacificus. J Kor Fish Soc 41: 7-12.
  5. Bergaman I, Loxley R. 1963. Two improved and simplified methods for the spectrophotometric determination of hydroxyproline. Anal Chem 35: 1961-1963.
  6. Matsui T, Matsufuji H, Seki E, Osajima K, Nakashima M, Osajima Y. 1993. Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates deived from sardine muscle. Biosci Biotech Biochem 57: 922-925.
  7. AOAC. 1990. Official methods of analysis. 15th ed. Association of Official Analytical Chemists, Washington, DC, USA. p 777-784.
  8. Lowry OH, Rosebrough NJ, Farr AL, Randall RL. 1951. Protein measurement with folin phenol reagent. J Biol Chem 193: 265-275.
  9. Lee EJ, Kim JS, Kwon JH. 2008. Optimization of microwave- assisted extraction conditions for total catechin and electron donating ability of grape seed extracts. Korean J Food Preserv 15: 840-846.
  10. Marklund G, Marklund S. 1975. Involvement of superoxide anion radical in the oxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 47: 469-474.
  11. Martinez-Esparaza M, Jimenez-Cervantes C, Solano F, Lozano JA, Garcia-Borron JC. 1998. Mechanism of melanogenesis inhibition by tumor necrosis factor-alpha in B16/F10 mouse melanoma cells. Eur J Biochem 255: 139-146.
  12. Quan T, He T, Voorhees JJ, Fisher GJ. 2001. Ultraviolet irradiation blocks cellular responses to transforming growth factor-beta by down-regulating its type II receptor and inducing Smad7. J Biol Chem 276: 26349-26356.
  13. Chiang HM, Lin TJ, Chiu CY, Chang CW, Hsu KC, Fan PC, Wen KC. 2011. Coffea arabica extract and its constituents prevent photoaging by supressing MMPs expression and MAP kinase pathway. Food Chem Toxicol 49: 309-318.
  14. Lee JH, Seo JH, Park YH, Kim WG, Lim KM, Lee SJ. 2008. The effect of hydroxyproline and Pro-Hyp dipeptide on UV-damaged skin of hairless mice. Korean J Food Sci Technol 40: 436-442.
  15. Choi YC. 2013. Development of high pressure/high temperature processing and high pressure enzymatic processing for rapid hydrolysis of porcine placenta. MS Thesis. Konkuk University, Seoul, Korea. p 3.
  16. Harris JR. 1990. Gelatin in press food gels. Johnston-Banks FA, ed. Elsevier Applied Science Publishers, London, UK. p 233-289.
  17. Perlish JS, Lemlich G, Fleischmajer R. 1998. Identification of collagen fibrils in scleroderma skin. J Invest Dermatol 90: 48-54.
  18. Kim SK, Yang HP, Lee EH. 1991. The development of a natural seasoning using the enzymatic hydrolysate of fish skin. Korean J Biotechnol Bioeng 6: 327-336.
  19. Kim JW, Kim DK, Kim MJ, Kim SD. 2010. Extraction and bleaching of acid- and pepsin-soluble collagens from shark skin and muscle. Korean J Food Preserv 17: 91-99.
  20. Weiss JB, Ayad S. 1982. An introduction to collagen. In Collagen in Health and Disease. Churchill Livingstone, New York, NY, USA. p 1-17.
  21. McCormick RJ. 1994. Structure and properties of tissues. In Muscle Foods, Meat Poultry and Seafood Technology. Chapman and Hall, New York, NY, USA. p 25-62.
  22. Wood A, Ogawa M, Portier RJ, Schexnayder M, Shirley M, Losso JN. 2008. Biochemical properties of alligator (Alligator mississippiensis) bone collagen. Biochem Physiol 151: 246-249.
  23. Gilsenan PM, Ross-Murphy SB. 2000. Rheological characterization of gelatins from mammalian and marine sources. Food Hydrocolloids 90: 191-195.
  24. Ha YK. 2009. Development and evaluation of functional ingredient using Jellyfish (Rhopilema esculentum). MS Thesis. Andong National University, Andong, Korea. p 50-51
  25. Matmaroh K, Benjakul S, Prodpran T, Encarnacion AB, Kishimura H. 2011. Characteristics of acid soluble collagen and pepsin soluble collagen from scale of spotted golden goatfish (Parupeneus heptacanthus). Food Chem 129: 1179-1186.
  26. Yamaguchi K, Lavety J, Love RM. 1976. The connective tissues of fish: Ⅷ. Comparative studies on hake, cod and catfish collagens. Int J Food Sci Technol 11: 389-399.
  27. Bell J, Brodsky B, Berman HM. 1995. Hydration structure of a collagen peptide. Structure 3: 893-906.
  28. Muyonga JH, Cole CGB, Duu KG. 2004. Characterisation of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus). Food Chem 85: 81-89.
  29. Kim JW, Kim DK, Park JS, Lee YK, Beik KY, Kim SD. 2009. Antioxidant and antimicrobial activities of shark collagens, and inhibitory actions on elastase and tyrosinase. Korean J Food Preserv 16: 419-426.
  30. Kim SK, Lee HC, Byun HC, Jeon YJ. 1996. Isolation and characterization of antioxidative peptides from enzymatic hydrolysated of tellowfin sole skin gelatin. J Korean Soc Fish 29: 246-255.
  31. Kim SJ, Kim JD, Kang MJ, Ahn HY, Kim DJ. 2000. Collagen- induced activation of MMPs (membrane-type matrix metalloproteinase and matrix metalloproteinase-2) in ovarian cancer cell lines in vitro. J Korean Soc Obstet Gynacol 43: 1972-1978.
  32. Kwon MC, Kim CH, Kim HS, Syed AQ, Hwang BY, Lee HY. 2007. Anti-wrinkle activity of low molecular weight peptides derived from the collagen isolated from Asterias amurensis. Korean J Food Sci Technol 39: 625-629.

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