Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
권호 표지
DOI QR코드

DOI QR Code

Characterization of Acid- and Pepsin-soluble Collagens from Rockfish Sebastes schlegeli Skin

  • Kim, Hyung-Jun (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University) ;
  • Jee, Seong-Joon (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University) ;
  • Yoon, Min-Suck (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University) ;
  • Youn, Mu-Ho (General Marine Product Processing Factory, Geoje Federation of Fisheries Cooperatives) ;
  • Kang, Kyung-Tae (Hansung Enterprise Co., LTD) ;
  • Lee, Dong-Ho (The Bureau of Risk Management, Korea Food & Drug Administration) ;
  • Heu, Min-Soo (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University) ;
  • Kim, Jin-Soo (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University)
  • Published : 2009.03.31
Download PDF
⟨ Previous Next ⟩

Abstract

Biochemical and functional properties of acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from rockfish skin were characterized. Yield of PSC (90.0%) was higher than that of ASC (63.2%). Both ASC and the PSC consisted of ${\alpha}1$ and ${\alpha}2$ chains, and $\alpha$-cross-linked components. According to the results of hydroxylation of proline and lysine, and FT-IR, no difference between the helical structure of ASC and PSC was identified. Thermal denaturation temperature (TDT) of ASC from rockfish skin was $22.8^{\circ}C$, the same as exhibited in PSC. Both ASC and PSC were higher in water absorption capacity (WAC) and oil absorption capacity (OAC) than other vegetable proteins. According to the results of emulsifying activity (EA) and cooking stability (CS), both ASC and PSC from rockfish skin were inferior compared to the commercial emulsifier (Tween-80). The results of FT-IR suggested that the structure of PSC was slightly different when compared to that of ASC. No differences in solubility were established between ASC and PSC from rockfish skin at various pH and NaCl concentrations.

Keywords

References

  1. AOAC. 1995. Official Methods of Analysis. 16th ed. Association of Official Analytical Chemists, Washington DC., USA, 69-74
  2. Beuchat, L.R. 1981. Functional and electrophoretic characteristics of succinylated peanut flour proteins. J. Agric. Food Chem., 46, 71-75
  3. Bligh, E.G. and W.J. Dyer. 1959. A rapid method of lipid extraction and purification. Can. J. Biochem. Physiol., 37, 911-917 https://doi.org/10.1139/y59-099
  4. Burghagen, M. 1999. Meat. In: Food Chem. 2nd ed. Belitz, H.D. and W. Grosch. Springer-Verlag. Berlin, Germany, 527-580
  5. Ciarlo, A.S., M.E. Paredi and A.N. Fraga. 1997. Isolation of soluble collagen from hake skin (Merluccius hubbsi). J. Aquatic. Food Product. Technol., 6, 65-77 https://doi.org/10.1300/J030v06n01_06
  6. Codex Code. 2004. European Community Comments for the Codex Committee on Food Additives and Contaminants- agenda Item 15(a) and 16(f), The JointFQA/THO Food Standards Propramme. Food Standards Propramme, Rome, Italy.
  7. Foegeding, E., T.C. Lanier and H.O. Hultin. 1996. Characteristics of edible muscle tissue. In: Food Chemisty. 3rd. ed. Fennema, O.R., ed. Academic Press, New York, USA, 879-942
  8. Gildberg, A. 2004. Enzymes and bioactive peptide from fish wastε related to fish silage, fish feed and fish sauce production. J. Aquatic Food Products Technology. 13, 3-11 https://doi.org/10.1300/J030v13n02_02
  9. Gomez-Guillen, M.C., J. Tumay, M.D. Femandez-Diaz, N. Ulmo, M.A. Lizarbe and P. Montero. 2002. Structural and physical properties of gelatin extracted fromdifferent marine species: a comparative study. Food Hydrocoll.;16, 25-34 https://doi.org/10.1016/S0268-005X(01)00035-2
  10. Hwang, J.H., S. Miuta, Y. Yokoyama and R. Yoshinaka. 2007. Purification and characterization of molecular spεcies of collagen in the skin of skate (Raja kenojei). Food Chem., 100, 921-925 https://doi.org/10.1016/j.foodchem.2005.10.046
  11. Jackson, M., L. Choo, P.H. Watson, W.C. Halliday and H.H. Mantsch. 1995. Beware of connective tissue protεins: assignment and implications of collagen absorptions in infrared spectra of human tissues. Biochima et Biophysica Acta., 1270, 1-6 https://doi.org/10.1016/0925-4439(94)00056-V
  12. Jongjareonrak, A., S. Benjakul, W. Visessanguan, T. Nagai and M. Tanaka. 2005. Is01ation and characterisation of acid and pepsin-s01ubilised collagens from the skin of Brownstripe red snapper (Lutjanus vitta). Food Chem., 93, 475-484 https://doi.org/10.1016/j.foodchem.2004.10.026
  13. KFDA (Korean Food and Drug Administration). 2006. Food Code. Moon-Yeoung Publishing Co., Seoul, Korea, 70-72
  14. Kim, J.S. and J.W. Park. 2004. Characterization of acidsoluble collagen from Pacific whiting surimi processing byproducts. J. Food Sci., 69C, 637-642
  15. Kim, J.S. and S.Y. Cho. 1996. Screening for raw material of modified gelatin in marine animal skins caught in coastal offshore water in Korea. Agricultural Chemistry and Biotechnology, 39, 134-139
  16. Kim, J. S., D.M. Yeum, H.G. Kang, I.S. Kim, C.S. Kong, T.G. Lee and M.S. Heu. 2002. Fundamentals and Applications for Canned Foods. Hyoil Publishing Co., Seoul, South Korea, 94-96, 276-277, 351-354
  17. Kimura, S., X.P. Zhu, R. Matsui, M. Shijoh and S. Takamizawa. 1988. Characterization of fish muscle type I collagen. J. Food Sci., 53, 1315-1318 https://doi.org/10.1111/j.1365-2621.1988.tb09266.x
  18. Kimura, S. 1992. Wide distribution of the type I collagen $\alpha_3$ chain in bony fish. Comp. Biochem. Physiol., 102B, 255-260 https://doi.org/10.1016/0305-0491(92)90119-C
  19. Kittiphattanabawon, P., S. Benjakul, W. Visεssanguan， T. Nagai and M. Tanaka. 2005. Characterisation of acidsoluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chem., 89, 363-372 https://doi.org/10.1016/j.foodchem.2004.02.042
  20. Kristinsson, H.G. and B.A. Rasco. 2000. Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline protease. J. Agric. Food Chem., 48, 657-666 https://doi.org/10.1021/jf990447v
  21. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriopage $T_4$ Nature, 227, 680-685 https://doi.org/10.1038/227680a0
  22. Lowry, O.H., N.J. Rosebrough, A.L. Farr and R.J. Randall. 1951. Protein measurement with Folin phenol reagent. J. Bio. Chem., 193, 256-275
  23. Ministry of Social Welfarε of Japan. 1960. Guide to Experiment of Sanitary Infection. III. Volatilε basic nitrogen. Kenpakusha, Tokyo, Japan, 30-32
  24. Montero, P., F. Jimenez-Colmenero and J. Borderias. 1991. Effìect of pH and the presence of NaCl on some hydration properties of collagenous material fromtrout (Salmo indeus Gibb) muscle and skin. J. Agric.Food Chem., 38, 604-609 https://doi.org/10.1021/jf00093a004
  25. Muyonga, J.H., C.G.B. Cole and K.G. Duodu. 2004a.Characterisation of acid s이uble collagen from skins ofyoung and adult Nile perch (Lates niloticus). Food.Chem., 85, 81-89 https://doi.org/10.1016/j.foodchem.2003.06.006
  26. Muyonga, J.H., C.G.B. Cole and K.G. Duodu. 2004b Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins andbones ofyoung and adult Nile perch (Lates niloticus). Food Chem., 86, 325-332 https://doi.org/10.1016/j.foodchem.2003.09.038
  27. Nagai, T. and N. Suzuki. 2000. Isolation of collagen from fish waste material-skin, bone and fins. Food Chem., 68, 277-281 https://doi.org/10.1016/S0308-8146(99)00188-0
  28. Nagai, T. and N. Suzuki. 2002. Preparation and partial characterization of collagen from paper nautilus (Argo nauta argo, Linnaeus) outer skin. Food Chem., 76, 149-153 https://doi.org/10.1016/S0308-8146(01)00255-2
  29. Nagai, T., M. Izumi and M. Ishii. 2004. Fish scale collagen preparation and partial characterization. Int. J. Food Sci. Technol., 39, 239-244 https://doi.org/10.1111/j.1365-2621.2004.00777.x
  30. Ogawa, M., J.R. Portier, M.W. Moody, J. Bell，M.A. Schexnayder and J.N. Losso. 2004. Biochemical properties of bone and scale collagens isolated ftomthε subtropical fish black drum (Pogonia cromis) and sheopshead seabream (Archosargus probatocephalus). Food Chem., 88, 495-501 https://doi.org/10.1016/j.foodchem.2004.02.006
  31. Ogawa, M., M.W. Moody, R.J. Portier, J. Bell, M.A. Schexnayder and J.N. Losso. 2003. Biochemical properties of black drum and sheepshεad seabreamskin collagen. J. Agric. Food Chem.. 51 , 8088-8092 https://doi.org/10.1021/jf034350r
  32. Park, C.H., J.H. Lee， K.T. Kang, J.W. Park and J.S. Kim. 2007. Characterization of acid-soluble collagen ftom Alaska pollock surimi processing by-products (refiner discharge). Food Sci. Biochem., 16, 549-556
  33. Sathe, S.K. and D.K. Salunkhe. 1981. Functional properiles of the great nothem bean (Phaseolus vulgaris L.) proteins: emulsioning， foaming, viscosity, andgelation properties. J. Food Sci., 46, 71-74 https://doi.org/10.1111/j.1365-2621.1981.tb14533.x
  34. Tsutagawa, Y., Y. Hosogai and H. Kawai. 1994. Comparison of mineral and phosphorus contents of muscle and bone in the wild and cultured horse mackεrel. J. FoodHyg. Soc. Japan, 34, 315-318
  35. Vojdani, F. 1996. Solubility. In: Methods of Testing Protein Fimctionality. 1st ed. Hall, G.M., ed. St Edmundsbury Press, London, UK, 11-60
  36. Wang，J.C. and J.E. Kinsella. 1976. Functional propertleS of novel proteins : alfalfa leaf protein. J. Food Sci., 41, 286-292 https://doi.org/10.1111/j.1365-2621.1976.tb00602.x
  37. Wang, L., X. An, Z. Xin, L. Zaho and Q. Hu. 2007. Isolation and characterization of collagen from the skin of deep-sea redfish (Sebastes mentella). J. FoodSci., 72, E450-E455 https://doi.org/10.1111/j.1750-3841.2007.00478.x
  38. Yang, J.S. 1997. Applications of gelatin in food and biotechnology. J. Food Sci. Nutr., 2, 263-268
  39. Yim, M.H. and J.H. Lee. 2000. Functional properties of fractionated soy protεin isolates by proteases from meju. J. Food Sci. Biotechnol., 9, 253-257
  40. Zhu, X.P. and S. Kimura. 1991. Thermal stability and subunit composition of muscle and skin type I collagens from skipjack. Nippon Suisan Gakkashi, 57, 755-760 https://doi.org/10.2331/suisan.57.755

Cited by

  1. 해파리의 식품성분 특성과 이의 유효 이용 vol.47, pp.5, 2009, https://doi.org/10.5657/kfas.2014.0459
  2. Comparison of collagen characteristics of sea- and freshwater-rainbow trout skin vol.25, pp.1, 2009, https://doi.org/10.1007/s10068-016-0020-z
  3. 넙치(Paralichthys olivaceus) 및 가다랑어(Katsuwonus pelamis) 알로부터 알칼리 가용화과정을 통해 회수한 알칼리 불용성획분의 이화학적 성분특성 vol.51, pp.3, 2009, https://doi.org/10.5657/kfas.2018.0230