Fisheries and Aquatic Sciences

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

DOI QR Code

Antioxidant and Cholinesterase Inhibitory Activities of Aqueous Extract from Rainbow Trout Oncorhynchus mykiss

  • Baek, Jae-Min (Central Regional Inland Fisheries Research, National Fisheries Research & Development Institute) ;
  • Yoon, Na-Young (Food and Safety Division, National Fisheries Research & Development Institute) ;
  • Kim, Yeon-Kye (Food and Safety Division, National Fisheries Research & Development Institute) ;
  • Lee, Doo-Seog (Food and Safety Division, National Fisheries Research & Development Institute) ;
  • Yoon, Ho-Dong (Food and Safety Division, National Fisheries Research & Development Institute) ;
  • Park, Jeung-Sook (Central Regional Inland Fisheries Research, National Fisheries Research & Development Institute)
  • Received : 2010.11.18
  • Accepted : 2011.05.16
  • Published : 2011.06.30
Download PDF
⟨ Previous Next ⟩

Abstract

We investigated the antioxidant and cholinesterase inhibitory activities of the aqueous extract of rainbow trout Oncorhynchus mykiss. The antioxidant activity of O. mykiss aqueous extract was determined by in vitro peroxynitrite scavenging activity and reducing power assays. The aqueous extract of O. mykiss showed potent peroxynitrite radical scavenging activity ($IC_{50}=0.12{\pm}0.001\;mg/mL$) and reducing power (absorbance=$0.47{\pm}0.001$) at the concentration of 1 mg/mL. The in vitro cholinesterase inhibitory activity of O. mykiss aqueous extract was examined using spectrophotometric analyses of acetyl- and butyrylcholinesterase. The aqueous extract of O. mykiss showed acetylcholinesterase inhibitory activity ($IC_{50}=1.61{\pm}0.13\;mg/mL$), but did not exhibit inhibitory activity against butyrylcholinesterase. These results suggest that O. mykiss possesses antioxidant and acetylcholinesterase inhibitory activities and provide scientific evidence for the health benefits of O. mykiss aqueous extract.

Keywords

References

  1. Association of Official Analytical Chemists. 1995. Official Methods of Analysis. 16th ed. Association of Official Analytical Chemists, Washington, DC, US, pp. 49-59.
  2. Atif F, Kaur M, Yousuf S and Raisuddin S. 2006. In vitro free radical scavenging activity of hepatic matallothionein induced in an Indian freshwater fish, Channa punctata Bloch. Chem Biol Interact 162, 172-180. https://doi.org/10.1016/j.cbi.2006.06.006
  3. Bachman DL, Wolf PA, Linn R, Knoefel JE, Cobb J, Belanger A, D'Agostino RB and White LR. 1992. Prevalence of dementia and probable senile dementia of the Alzheimer type in the Framingham study. Neurololgy 42, 115-119. https://doi.org/10.1212/WNL.42.1.115
  4. Behnke RJ. 1992. Native Trout of Western North America. American Fisheries Society Monograph 6, Bethesda, MD, US, pp. 1-275.
  5. Choi CS, Eom SH, Lee MS and Kim YM. 2010. Effect of an astaxanthin-supplemented diet on the nutritional composition of rainbow trout (Oncorhynchus mykiss). Kor J Fish Aquat Sci 43, 109-116. https://doi.org/10.5657/kfas.2010.43.2.109
  6. Ellman GL, Courtney KD, Andres V Jr and Featherstone RM. 1961. A new and rapid colorimetric deter-mination of acetylcholinesterase activity. Biochem Pharmacol 7, 88-95. https://doi.org/10.1016/0006-2952(61)90145-9
  7. Giacobini E. 2004. Drugs that target cholinesterase. In: Cognitive Enhancing Drugs. Buccafusco JJ, ed. Birkhauser-Verlag, Basel, CH, pp. 11-36.
  8. Kim KS and Choi YJ. 1993. Food components of coho salmon and rainbowtrout. Korean J Food Nutr 6, 73-80.
  9. Kooy NW, Royall JA, Ischiropoulos H and Beckman JS. 1994. Peroxynitrite-mediate oxidation of dihydrorhodamine 123. Free Radic Biol Med 16, 146-156.
  10. Lim GP, Calon F, Morihara T, Yang F, Teter B, Ubeda O, Salem N Jr, Frautschy SA and Cole GM. 2005. A diet enriched with omega-3 fatty acid docosahexaenoic acid reduces amyloid burden in an aged Alzheimer mouse model. J Neurosci 25, 3032-3240. https://doi.org/10.1523/JNEUROSCI.4225-04.2005
  11. Matsuno T, Katsuyama M and Nagata S. 1980. Comparative biochemical studies of carotenoids in fishes-XIX, carotenoids of chum salmon, coho salmon, biwa trout, red-spotted masu salmon, masu salmon and kokanee. Bull Jpn Soc Sci Fish 46, 879-884. https://doi.org/10.2331/suisan.46.879
  12. Oh HT, Kim SH, Choi HJ, Chung MJ and Ham SS. 2008. Antioxidative and antimutagenic activities of 70% ethanol extract from masou salmon (Oncorhynchus masou). Toxicol In Vitro 22, 1484-1488. https://doi.org/10.1016/j.tiv.2008.05.002
  13. Oh HT, Chung MJ, Kim SH, Choi HJ and Ham SS. 2009. Masou salmon (Oncorhynchus masou) ethanol extract decreases 3-hydroxy-3-methylglutaryl coenzyme A reductase expression in diet-induced obese mice. Nutr Res 29, 123-129. https://doi.org/10.1016/j.nutres.2008.11.006
  14. Oyaizu M. 1986. Studies on products of browning reaction: antioxidative activities of products of browning reaction prepared from glucosamine. Jpn J Nutr 44, 307-315. https://doi.org/10.5264/eiyogakuzashi.44.307
  15. Sastre J, Pallardo FV and Vina J. 2000. Mitochondrial oxidative stress plays a key role in aging and apoptosis. IUBMB Life 49, 427-435. https://doi.org/10.1080/152165400410281
  16. Schneider LS. 2001. Treatment of Alzheimer's disease with cholinesterase inhibitors. Clin Geriatr Med 17, 337-358. https://doi.org/10.1016/S0749-0690(05)70072-0
  17. Silman I and Sussman JL. 2005. Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology. Curr Opin Pharmacol 5, 293-302. https://doi.org/10.1016/j.coph.2005.01.014
  18. Singh N and Rajini PS. 2004. Free radical scavenging activity of an aqueous extract of potato peel. Food Chem 85, 611-616. https://doi.org/10.1016/j.foodchem.2003.07.003
  19. Squadrito GL and Pryor WA. 1998. Oxidative chemistry of nitric oxide: the roles of superoxide, peroxynitrite, and carbon dioxide. Free Radic Biol Med 25, 392-403. https://doi.org/10.1016/S0891-5849(98)00095-1
  20. Yu Q, Holloway HW, Utsuki T, Brossi A and Greig NH. 1999. Synthesis of novel phenserine-based-selective inhibitors of butyrylcholinesterase for Alzheimer's disease. J Med Chem 42, 1855-1861. https://doi.org/10.1021/jm980459s