Fisheries and Aquatic Sciences

한국수산과학회 (The Korean Society of Fisheries and Aquatic Science)
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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)
  • 투고 : 2010.12.29
  • 심사 : 2011.03.09
  • 발행 : 2011.03.31
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초록

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.

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  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
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  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