Fisheries and Aquatic Sciences

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

DOI QR Code

Fractionation of Gelatin Hydrolysates with Antioxidative Activity from Alaska Pollock Surimi Refiner Discharge

  • Park, Chan-Ho (Dept. of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Kim, Hyung-Jun (Dept. of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Kang, Kyung-Tae (Korea Health Industry Development Institute) ;
  • Park, Joo-Dong (CJ Cheiljedang Co.) ;
  • Heu, Min-Soo (Dept. of Nutrition and Food Science/Institute of Marine Industry, Gyeongsang National University) ;
  • Park, Jae-W. (Seafood Laboratory & Dept. of Food Science and Technology, Oregon State University) ;
  • Kim, Jin-Soo (Dept. of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University)
  • Published : 2009.09.30
Download PDF
⟨ Previous Next ⟩

Abstract

This study was conducted to obtain the gelatin fraction with a high anti oxidative activity from Alaska pollock surimi by-products using a two-step enzymatic hydrolysis and ultrafiltration. Among gelatin hydrolysates from refiner discharge of Alaska Pollock surimi, the highest antioxidative activity (81.5%) resulted from gelatin hydrolysate sequentially treated with Pronase E and Flavourzyme each for 2 hr. However, no difference was seen in the anti oxidative activity of the second hydrolysate (Pronase E-/Flavourzyme-treated hydrolysate) when compared to the permeate fractionated through a 10-kDa membrane. The results suggest that the Pronase E-/Flavourzyme-treated hydrolysate from refiner discharge gelatin of Alaska pollock surimi can be used as a supplementary raw material for improving health functionality.

Keywords

References

  1. Byun, H.G. and S.K. Kim. 2001. Purification and characterization of angiotensin converting enzyme (ACE) inhibitory peptides from Alaska pollock (Theragra chalcogramma) skin. Process. Biochemistry, 36, 1155-1162
  2. Chen, H.M., K. Muramoto and F. Yamauchi. 1995. Structural analysis of antioxidative peptides from soybean $\beta$-conglycinin. J. Agric. Food Chem., 43, 574-578 https://doi.org/10.1021/jf00051a004
  3. Cho, S.M., K.S. Kwak, D.C. Park, Y.S. Gu, c.l. Ji, D.H. Jang, Y.B. Lee and S.B. Kim. 2004. Processing optimization and functional properties of gelatin from shark (lsurus oxyrinchus) cartilage. Food Hydrocolloids., 18, 573-579 https://doi.org/10.1016/j.foodhyd.2003.10.001
  4. Cho, S.M., Y.S. Gu and S.B. Kim. 2005. Extracting optimization and physical properties ofyellowfin tuna (Thμnnus albacares) skin gelatin compared to mammalian gelatins. Food Hydrocolloids., 19, 221-229 https://doi.org/10.1016/j.foodhyd.2004.05.005
  5. Ciarlo, A.S., M.E. Paredi and A.N. Fraga. 1997. Isolation of soluble collagen from hake skin (Merluccius hubbsi). J. Aquatic Food Prod. Technol., 6, 65-77 https://doi.org/10.1300/J030v06n01_06
  6. Gbogouri, G.A., M. Linder, J. Fanni and M. Parmentier. 2004. Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates. J. Food Sci., 69, C615-C622 https://doi.org/10.1111/j.1365-2621.2004.tb09909.x
  7. Haug, I.J., K.I. Draget and O. Smidsrod. 2004. Physical and rheological propertiεs of fish gelatin compared to mammalian gelatin. Food Hydrocolloids, 18, 203-213 https://doi.org/10.1016/S0268-005X(03)00065-1
  8. Hoyle, N. and J .H. Merritt. 1994. Quality of fish protein hydrolysates from hεrring (Clupεa harengus). J. Food Sci., 59, 76-79, 129 https://doi.org/10.1111/j.1365-2621.1994.tb06901.x
  9. Jamilah, B. and K.G. Harvinder. 2002. Properties of gelatins from skins of fish-black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica). Food Chem., 77, 81-84 https://doi.org/10.1016/S0308-8146(01)00328-4
  10. Jeon, Y.J., H.G. Byun and S.K. Kim. 1999. Improvement of functional properties of cod frame protein hydroIysates using ultrafiltration membranes. Process Biochem., 35, 471-478 https://doi.org/10.1016/S0032-9592(99)00098-9
  11. Marcuse, R. 1962. The effect of some amino acids on the oxidation of linoleic acid and its methyl ester. J. Am. Oil Chem. Soc., 39, 97-103 https://doi.org/10.1007/BF02631680
  12. Mitsuda, H., K. Yasumoto and K. Iwami. 1966. Antioxidative action of indole compounds during the autooxidation of linoleic acid. Eiyo to Syokuryo, 19, 210-214 https://doi.org/10.4327/jsnfs1949.19.210
  13. Karrel, M., S.R. Tannenbaum, D.H Wallace and H. Maloney. 1966. Autooxidation of methyl linoleate m freeze dried mode J systems. EffIects of added amino acids. J. Food Sci., 31 , 892-896 https://doi.org/10.1111/j.1365-2621.1966.tb03266.x
  14. Kim, S.K., H.G. Byun, Y.J. Jeon and D.J. Cho. 1994. Functional propεrties of fish skin gelatin hydrolysate from a continuous two-stage membrane reactor. Korean Agric. Chem. Biotechnol., 37, 85-93
  15. Kim, S.K., H.G. Byun, P.J. Park and F. Shahidi. 2001a.Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate. J. Agric. Food Chem., 49, 2992-2997 https://doi.org/10.1021/jf001119u
  16. Kim, S.K., Y.T. Kim, H.G. Byun, K. S. Nam, D.S. Joo and F. Shahidi. 2001b. Isolation and characterization of antioxidativε peptides from gealtin hydrolysate of Alaska pollack skin. J. Agric. Food Chem., 49, 1984-1989 https://doi.org/10.1021/jf000494j
  17. Korhonen, H., A. Pihlanto-Leppala, T. Tupasεla. 1998. lmpact of processing on bioactive proteins and peptides. Trends Food Sci. Technol., 9, 307-319 https://doi.org/10.1016/S0924-2244(98)00054-5
  18. Morrissey, M.T., J.W. Park and L. Huang. 2000. Surimi processing waste-its control and utilization. In: Surimi and Surimi Seafoods. editor Park JW. New York and Bassel Marcel Dekker, 127-165
  19. Mendis, E., N. Rajapakse and S.K. Kim. 2005. Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. J. Agric. Food Chem., 53, 581-587 https://doi.org/10.1021/jf048877v
  20. Park, C.H. 2006. Functional properties and utilization of collagen and gelatin from surimi by-products, refiner discharge. (MSci thesis) Gyeongsang National Universíty. Tongyeong, Korea
  21. Park, C.H., J.H. Lee, K.T. Kang, J.W. Park and J.S. Kim. 2007. Characterization of acid-soluble collagen from Alaska pollock surimi processing by-products (refiner discharge). Food Sci. Biotechnol., 16, 549-556
  22. Steel, R.G.D. and J.H. Torrie. 1980. Principle and procedures of statistics. 1st ed. Tokyo. McGraw-Hill Kogakusha, 187-221
  23. Uchida, K. and S. Kawakishi. 1992. Sequence dependent reactivity of histidine-containing peptides with copper (lI) ascorbate. J. Agric. Biol. Chem., 40, 13-16 https://doi.org/10.1021/jf00013a003
  24. Wendel, A.P. 1999. Recovery and utilization of Pacific whiting frame meat for sunml production. (MSci thesis) Oregon State University. Corvallis, Oregon, USA
  25. Wu, H.C., H.M. Chen and C.Y. Shiau. 2003. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Research Intemational., 36, 949-957 https://doi.org/10.1016/S0963-9969(03)00104-2
  26. Yamaguchi, N. 1971. Studies on antioxidative activities of amino compounds on fats and oils. Part I. Oxidation of methionine during course of autooxidation of Iinoleic acid. Nippon Shokuhin Kogyo Gakkaishi, 18, 313-318 https://doi.org/10.3136/nskkk1962.18.313