DOI QR코드

DOI QR Code

Antioxidant and ACE Inhibiting Activities of the Rockfish Sebastes hubbsi Skin Gelatin Hydrolysates Produced by Sequential Two-step Enzymatic Hydrolysis

  • Kim, Hyung-Jun (Children's Dietary Life Safety Division, Korea Food & Drug Administration) ;
  • Park, Kwon-Hyun (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Shin, Jun-Ho (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Lee, Ji-Sun (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Heu, Min-Soo (Department of Food Science and Nutrition/Institute of Marine Industry, Gyeongsang National University) ;
  • Lee, Dong-Ho (Children's Dietary Life Safety Division, Korea Food & Drug Administration) ;
  • Kim, Jin-Soo (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University)
  • Received : 2010.12.29
  • Accepted : 2011.03.09
  • Published : 2011.03.31

Abstract

This study was conducted to obtain hydrolysates with potent antioxidative activity from rockfish skin gelatin. Gelatin was extracted under high temperature/high pressure using a two-step enzymatic hydrolysis with commercial enzymes such as Alcalase, Flavourzyme, Neutrase, and Protamex. The second rockfish-skin gelatin hydrolysate (SRSGH) was prepared by further incubating the first gelatin hydrolysate (FRSGH), which had been hydrolyzed with Alcalase for 1-h (FRSGH-A1), with Flavourzyme for 2-h (SRSGH-F2). The second gelatin hydrolysate showed higher antioxidative activity of 3.72 as measured by a Metrohm Rancimat and superior angiotensin I-converting enzyme (ACE) inhibiting activity of 0.82 mg/mL. Compared with the gelatin, the relative proportion in SRSGH-F2 was markedly decreased in the 100-kDa peak, whereas it was increased in that less than 100-kDa. The amino acid composition of SRSGH-F2 was rich in glycine (25.9%), proline (10.8%), alanine (9.1%), and glutamic acid (9.1%). In contrast, it was poor in cystine (not detected), methionine (1.6%), tyrosine (0.4%), hydroxylysine (0.9%), and histidine (0.9%). In recent years, demand for natural functional foods has been increasing, and SRSGH-F2 can be used as a functional food ingredient in the food industries. However, further detailed studies on SRSGH-F2 with regard to its antioxidant activity in vivo and the various antioxidant mechanisms are needed.

Keywords

References

  1. Becker GL. 1993. Preserving food and health: antioxidants make fuctional, nutritious preservatives. Food Process 4, 885-889.
  2. Byun HG and Kim SK. 2001. Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollock (Theragra chalcogramma) skin. Process Biochemistry 36, 1155-1162. https://doi.org/10.1016/S0032-9592(00)00297-1
  3. Chang CY, Wu KC and Chiang SH. 2007. Antioxidant properties and protein compositions of porcine haemoglobin hydrolysates. J Food Chem 100, 1537-1543. https://doi.org/10.1016/j.foodchem.2005.12.019
  4. Fishery Production Survey. 2010. http://fs.fips.go.kr
  5. Frega N, Mozzon M and Lecker G. 1999. Effects of free fatty acids on oxidative stability of vegetable oil. J Agric Food Chem 47, 1035-1040. https://doi.org/10.1021/jf980496s
  6. Gbogouri GA, Linder M, Fanni J and Parmentier M. 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 IJ, Draget KI and Smidsrod O. 2004. Physical and rheological properties of fish gelatin compared to mammalian gelatin. Food Hydrocolloids 18, 203-213. https://doi.org/10.1016/S0268-005X(03)00065-1
  8. Hiramoto K, Jonkoh H, Sako KI and Kikugawa K. 1993. DNA breaking activity of the carbon-centered radical generated from 2,2'-azobis (2 amidinopropane) hydrochloride (AAPH). Free Radic Res Commun 19, 323-332. https://doi.org/10.3109/10715769309056521
  9. Horiuchi M, Fujimura KI, Terashima T and Iso T. 1982. Method for determination of angiotensin I converting enzyme activity in blood and tissue by high-performance liquid chromatography. J Chromatogr 233, 123-130. https://doi.org/10.1016/S0378-4347(00)81738-7
  10. Hoyle N and Merritt JH. 1994. Quality of fish protein hydrolysates from herring (Clupea harengus). J Food Sci 59, 76-79, 129. https://doi.org/10.1111/j.1365-2621.1994.tb06901.x
  11. Jamilah B and Harvinder KG. 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
  12. Jeon YJ, Byun HG and Kim SK. 1999. Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes. Process Biochem 35, 471-478. https://doi.org/10.1016/S0032-9592(99)00098-9
  13. Jun SY, Park PJ, Jung WK and Kim SK. 2004. Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. J Eur Food Res and Tech 219, 20-26. https://doi.org/10.1007/s00217-004-0882-9
  14. Karel M, Tannenbaum SR, Wallace DH and Maloney H. 1966. Autooxidation of methyl linoleate in freeze dried model systems. Effects of added amino acids. J Food Sci 31, 892-896. https://doi.org/10.1111/j.1365-2621.1966.tb03266.x
  15. Kim HJ, Jee SJ, Yoon MS, Youn MH, Kang KT, Lee DH, Heu MS and Kim JS. 2009. Characterization of acidand pepsin-soluble collagens from rockfish Sebastes schlegeli skin. J Fish Sci Tech 12, 6-15.
  16. Kim HJ, Yoon MS, Park KH, Shin JH, Heu MS and Kim JS. 2010. Processing optimization of gelatin from rockfish skin based on yield. Fish Aqua Sci 13, 1-11.
  17. Kim JS and Park JW. 2004. Characterization of acidsoluble collagen from Pacific whiting surimi processing byproducts. J Food Sci 69, C637-C642. https://doi.org/10.1111/j.1365-2621.2004.tb09912.x
  18. Kim SK, Byun HG, Jeon YJ and Cho DJ. 1994. Functional properties of fish skin gelatin hydrolysate from a continuous two-stage membrane reactor. Korean Agric Chem Biotechnol 37, 85-93.
  19. Kim SK, Byun HG, Park PJ and Shahidi F. 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
  20. Kim SK, Kim YT, Byun HG, Nam KS, Joo DS and Shahidi F. 2001b. Isolation and characterization of antioxidative peptides from gealtin hydrolysate of Alaska pollack skin. J Agric Food Chem 49, 1984-1989. https://doi.org/10.1021/jf000494j
  21. Kong CS, Kim JA, Qjan ZJ, Kim YA, Lee JI, Kim SK, Nam TJ and Seo Y. 2009. Protective effect of isorhamnetin 3-O-$\beta$-D-glucopyranoside from Salicornia herbacea against oxidation-ionduced cell damage. Food Chem Toxicol 47, 1914-1920. https://doi.org/10.1016/j.fct.2009.05.002
  22. Korhonen H, Pihlanto-Leppala A and Tupasela T. 1998. Impact of processing on bioactive proteins and peptides. Trends Food Sci Technol 9, 307-319. https://doi.org/10.1016/S0924-2244(98)00054-5
  23. Maillard MG, Soum MH, Meydani SN and Berset C. 1996. Antioxidant activity of barely and malt: relationship with phenolic content. Food Sci Tech 29, 238-244.
  24. 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
  25. Mendis E, Rajapakse N and Kim SK. 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
  26. Nanjo F, Goto K, Seto R, Suzuki M, Sakai M and Hara Y. 1996. Scavenging effects of tea catechins and their derivatives on 1,1-diphenyl-2-picrylhydrazyl radical. Free Radic Biol Med 21, 895-902. https://doi.org/10.1016/0891-5849(96)00237-7
  27. Qian ZJ, Jung WK and Kim SK. 2008. Free radical scavenging activity of a novel antioxidative peptide purified from hydrolysate of bullfrog skin, Rana catesbeiana Shaw. Biores Tech 99, 1690-1698. https://doi.org/10.1016/j.biortech.2007.04.005
  28. Rajapakse N, Mendis E, Jung WK, Je JY and Kim SK. 2005. Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties. Food Research International 38, 175-182. https://doi.org/10.1016/j.foodres.2004.10.002
  29. Rosen GM and Rauckman EJ. 1980. Spin trapping of superoxide and hydroxyl radicals. Method Enzymol 105, 198-209.
  30. Wu HC, Chen HM and Shiau CY. 2003. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber Austriasicus). Food Research International 36, 949-957. https://doi.org/10.1016/S0963-9969(02)00226-0
  31. Yamaguchi F, Ariga T, Yoshimira Y and Nakazawa H. 2000. Antioxidant and antiglycation of carcinol from Garcinia indica fruit rind. J Agric Food Chem 48,180-185. https://doi.org/10.1021/jf990845y
  32. Zhao BL, Li XJ, He R, Cheng SJ and Xin WJ. 1989. Scavenging effect of extracts of green tea and natural antioxidants on active oxygen radicals. Cell Biophys 14, 175-185. https://doi.org/10.1007/BF02797132

Cited by

  1. Fractionation and Characterization of Fractions with High Antioxidative Activity from the Gelatin Hydrolysates of Korean Rockfish Sebastes schlegelii Skin vol.14, pp.3, 2011, https://doi.org/10.5657/FAS.2011.0168
  2. Food Protein-Derived Bioactive Peptides: Production, Processing, and Potential Health Benefits vol.77, pp.1, 2012, https://doi.org/10.1111/j.1750-3841.2011.02455.x
  3. Strains for Proteolytic Enzymes Production by Solid State Fermentation vol.2016, pp.2090-0414, 2016, https://doi.org/10.1155/2016/3016149
  4. A Review of Protein Hydrolysates and Bioactive Peptides Deriving from Wastes Generated by Fish Processing vol.11, pp.1, 2018, https://doi.org/10.1007/s11947-017-1940-1
  5. Characterization and Antioxidant and Angiotensin I-Converting Enzyme (ACE)-Inhibitory Activities of Gelatin Hydrolysates Prepared from Extrusion-Pretreated Milkfish (Chanos chanos) Scale vol.16, pp.10, 2018, https://doi.org/10.3390/md16100346
  6. Protein Modification During Ingredient Preparation and Food Processing: Approaches to Improve Food Processability and Nutrition vol.7, pp.7, 2011, https://doi.org/10.1007/s11947-014-1326-6
  7. Protein Recovery from Underutilised Marine Bioresources for Product Development with Nutraceutical and Pharmaceutical Bioactivities vol.18, pp.8, 2011, https://doi.org/10.3390/md18080391
  8. Characterization of Protein Hydrolysates from Fish Discards and By-Products from the North-West Spain Fishing Fleet as Potential Sources of Bioactive Peptides vol.19, pp.6, 2011, https://doi.org/10.3390/md19060338