Journal
FOOD AND CHEMICAL TOXICOLOGY
Volume 52, Issue -, Pages 113-120Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fct.2012.10.058
Keywords
Flounder; Paralichthys olivaceus; Antioxidative peptide; Enzymatic hydrolysis; Radical scavenging; alpha-Chymotrypsin
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Funding
- National Research Foundation of Korea (NRF)
- Korea government (MEST) [2012H1B8A2025863]
- National Research Foundation of Korea [2012H1B8A2025863] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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We investigated the effects of bioactive-peptides from hydrolysates of flounder fish muscle (FFM) on antioxidant activity. The hydrolysates were prepared by enzymatic reactions of FFM using eight commercial proteases such as papain, pepsin, trypsin, neutrase, alcalase, kojizyme, protamex, and alpha-chymotrypsin. The alpha-chymotrypsin hydrolysate showed the strongest antioxidant activity among the eight enzymatic hydrolysates. Further separation of the alpha-chymotrypsin hydrolysate was performed by ultrafiltration, gel filtration, and reverse-phase high performance liquid chromatography. Consequently, two novel peptides with high antioxidant activity were purified, and their amino acid sequences were determined (Val-Cys-Ser-Val [VCSV] and Cys-Ala-Ala-Pro [CAAP], respectively). The two peptides showed good scavenging activity against the 1,1-diphenyl-2-picrylhydrazyl (DPPH) free radical (IC50 values, 111.32 and 26.89 mu M, respectively) and high cytoprotective activities against 2,2-azobis-(2-amidinopropane) dihydrochloride (AAPH) without cytotoxicity and scavenged total reactive oxygen species in Vero cells. In particular, apoptotic bodies produced by AAPH dose-dependently decreased following treatment with the CAAP peptide. These results revealed firstly the two peptides with strong antioxidative effects from FFM. (C) 2012 Elsevier Ltd. All rights reserved.
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