Journal of Marine Bioscience and Biotechnology (한국해양바이오학회지)

The Korean Society for Marine Biotechnology (한국해양바이오학회)
권호 표지
DOI QR코드

DOI QR Code

Development of Bioactive Substances from Fishery Processing by-products in Jeju

제주 수산가공부산물 유래 기능성 소재 탐색

  • Kang, Nalae (Department of Marine Life Sciences, Jeju National University) ;
  • Lee, WonWoo (Department of Marine Life Sciences, Jeju National University) ;
  • Ko, Ju-Young (Department of Marine Life Sciences, Jeju National University) ;
  • Kim, Hyun-Soo (Department of Marine Life Sciences, Jeju National University) ;
  • Kim, Junseong (Department of Marine Life Sciences, Jeju National University) ;
  • Ahn, Yong-Seok (Research Institute of Processing from Jeju Fisher Food, Choung Ryong Fisheries Co., LTD.) ;
  • Ko, Chang-Ik (Research Institute of Processing from Jeju Fisher Food, Choung Ryong Fisheries Co., LTD.) ;
  • Jeong, Joon Bum (Department of Marine Life Sciences, Jeju National University) ;
  • Jeon, You-Jin (Department of Marine Life Sciences, Jeju National University)
  • 강나래 (제주대학교 해양생명과학과) ;
  • 이원우 (제주대학교 해양생명과학과) ;
  • 고주영 (제주대학교 해양생명과학과) ;
  • 김현수 (제주대학교 해양생명과학과) ;
  • 김준성 (제주대학교 해양생명과학과) ;
  • 안용석 ((주) 청룡수산 수산식품가공연구소) ;
  • 고창익 ((주) 청룡수산 수산식품가공연구소) ;
  • 정준범 (제주대학교 해양생명과학과) ;
  • 전유진 (제주대학교 해양생명과학과)
  • Received : 2014.12.11
  • Accepted : 2014.12.22
  • Published : 2014.12.31
Download PDF
⟨ Previous Next ⟩

Abstract

In this study, we investigated the bioactive substances of the Alcalase hydrolysate obtained from fishery processing by-products in Jeju by measuring bioactivities including radical scavenging acitivty, cytoprotective activity against 2,2-azobis-(2-amidino-propane) dihydrochloride (AAPH), and ACE inhibitory activity. This study is important because of utilization of unused fishery processing by-products in Jeju. The Alcalase hydrolysate was prepared through the hot water extraction and enzymatic hydrolysis, and then further separation of the Alcalase hydrolysate was performed by ultrafiltration using 10 kDa molecular weight cut-off membrane. The Alcalase hydrolysate showed the relatively higher DPPH and peroxyl radical scavenging activity ($IC_{50}$ value; 1.30 mg/ml and 0.888 mg/ml, respectively). Also, the Alcalase hydrolysate showed the ACE inhibitory activity with 1.87 mg/ml of $IC_{50}$ value. These biological activities are increased over 1.2 or 2.5 times through the ultrafiltration of the Alcalase hydrolysate. Therefore, the Alcalase hydrolysate obtained from fishery processing by-products in Jeju and the different molecular weight fractions should be given consideration for food and cosmetics ingredient. Furthermore, this research on the utility of fishery processing by-products might be a useful tool into the industry.

Keywords

References

  1. Ahn, C. B. and Lee, E. H. 1992. Utilization of Chitin Prepared from the Shellfish Crust. Bull. Korean Fish. Soc. 25(1), 45-50.
  2. Ahn, Y. S., Lee, W. W., Lee, S. H., Ahn, G., Ko, C. I., Oh, C., Oh, M. C., Kim, D. W., Jeon, Y. J. and Kim, S. H. 2009. Angiotensin I Converting Enzyme Inhibitory Effects of Gelatin Hydrolysates Prepared from Tilapia mossambica Scales by Hot Water and Enzymatic Extraction. Korean J. Fish Aquat. Sci. 42(5), 426-433. https://doi.org/10.5657/kfas.2009.42.5.426
  3. Ahn, Y. S., Lee, W. W., Lee, S. H., Ahn, G., Ko, C. I., Oh, C., Oh, M. C., Kim, D. W., Jeon, Y. J. and Kim, S. H. 2009. Processing and Biological Activity of Gelatin Hydrolysate from Branchiostegus japonicus Scalse. Korean J. Fish Aquat. Sci. 42(5), 417-425.
  4. Cheung, H. S., Wang, F. I., Ondetti, M. A., Sabo, E. F. and Cushman, D. W. 1980. Binding of peptide substrates and inhibitors of angiotensin I-converting enzyme. Importance of the COOH-terminal dipeptide sequence. J. Biol. Chem. 225, 401-407.
  5. Choi, J., Kim, Y. J., Sung, N. Y., Kim, J. H., Ahn, D. H., Chun, B. S., Cho, K. Y., Byun, M. W. and Lee, J. W. 2009. Investigation on the Increase of Antioxidant Activity of Cooking Drip from Enteroctopus dofleini by Irradiation. J. Korean Soc. Food Sci. Nutr. 38(1), 121-124. https://doi.org/10.3746/jkfn.2009.38.1.121
  6. Do, J. R., Heo, I. S., Jo, J. H., Kim, D. S., Kim, H. K., Kim, S. S. and Han, C. K. 2006. Effect of antihyperteinsive peptides originated from various marine proteins on ACE inhibitory activity and systolic blood pressure in spontaneously hypertensive Rats. Korean J Food Sci. Technol. 38, 567-570.
  7. Kim, J. O. and Kang, S. K. 2011. Economic Impact Effect Analysis of Flounder Aquaculture Industry in Jeju. J. Fish. Bus. Adm. 42(1), 85-96.
  8. Kim, S. K. 2003. Development of Novel Bioactive Substances from Fishery Byproducts. Food Ind. Nutr. 8(3), 1-8.
  9. Ko, J. Y., Lee, J. H., Samarakoon, K., Kim, J. S. and Jeon, Y. J. 2013. Purification and determination of two novel antioxidant peptides from flounder fish (Paralichthys olivaceus) using digestive protease. Food Chem. Toxicol. 52, 113-120. https://doi.org/10.1016/j.fct.2012.10.058
  10. 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
  11. Park, S. H., Lee, J. K., Jeon, J. K. and Byun, H. G. 2011. Characterization of a Collagenase-1 Inhibitory Peptide Purified from Skate Dipturus chilensis Skin. Kor. J. Fish Aquat. Sci. 44(5), 456-463. https://doi.org/10.5657/KFAS.2011.0456
  12. StatisticsKorea. 2014. (http://www.index.go.kr/potal/main/EachDtlPageDetail.do?idx_cd=1317)
  13. StatisticsKorea. 2014. (http://www.index.go.kr/potal/main/EachDtlPageDetail.do?idx_cd=2748)