Purification and Characterization of Antioxidant Peptides from Oyster (Saccostrea cucullata) Hydrolysate and the Anticancer Activity of Hydrolysate on Human Colon Cancer Cell Lines
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The focus of the study was to investigate antioxidant activity and characterize antioxidant peptides from oyster (Saccostrea cucullata) protein hydrolysate. The protease hydrolysate of oyster exhibited strong potential to donate hydrogen and was able to scavenge Hydrogen peroxide, Hydroxyl and DPPH radicals. Due to the high antioxidant potential, hydrolysate was purified in Sephadex G-25 gel filtration chromatography. The active peptide fraction was further purified by UPLC-MS. Totally seven antioxidant peptides were collected. Among seven peptides (SCAP 1–7), three peptides (SCAP 1, 3 and 7) had highest scavenging ability on DPPH radicals. The amino acid sequence and molecular mass of purified antioxidant peptides (SCAP1, SCAP3 and SCAP7) were determined by Q-TOF ESI mass spectroscopy and structures of the peptides were Leu-Ala-Asn-Ala-Lys (MW = 515.29 Da), Pro-Ser-Leu-Val-Gly-Arg-Pro–Pro-Val-Gly-Lys-Leu-Thr-Leu (MW = 1,432.89 Da) and Val-Lys-Val-Leu-Leu-Glu-His-Pro-Val-Leu (MW = 1,145.75 Da), respectively. The oyster hydrolysate was tested for cell cytotoxicity on Vero (kidney epithelial cells of the African Green Monkey) and HT-29 (human colon carcinoma) cell lines. It was found that the hydrolysate did not show any cytotoxic effect for Vero cell lines and exerted a significant cytotoxic effect on HT-29 cell lines. We thus conclude that the anticancer and antioxidative hydrolysate from oyster (S. cucullata) may be useful ingredients in food and nutraceutical applications.
KeywordsOyster Saccostrea cucullata Enzymatic hydrolysis Protein hydrolysate Antioxidant peptide DPPH Electrospray ionization mass spectrometry
The authors would like to thank Ministry Of Earth Sciences for financial support, under the “Drugs from sea” programme and the authors are grateful to the authorities of Annamalai University for providing the necessary facilities.
Conflict of interest
S. Umayaparvathi, M. Arumugam, S. Meenakshi, G. Draeger, A. Kirschning and T. Balasubramanian declare that they have no conflict of interest.
Statement of informed consent/Human and animal rights
This article does not contain any studies with human or animal subjects performed by the any of the authors.
- AOAC (1990) Official methods of analysis. Association of Official Analytical Chemists, Washington, DCGoogle Scholar
- Huang DC, Li QF, Li P, Li XQ, Song YZ (2002) Effects of oyster low molecular weight bioactive substance on the human lung adenocarcinoma A549 cells. J Xiamen Univ 41:614–617Google Scholar
- Hunt DA, Miescier J, Redman J, Salinger A, Lucas JP (1984) Molluscan shellfish, fresh or fresh frozen oysters, mussels or clams. In: Speck ML (ed) Compendium of methods for the microbiological examination of foods, 2nd edn. American Public Health Association, Washington, DCGoogle Scholar
- Kembhavi AA, Kulkarni A, Pant A (1993) Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No. 64. Appl Biochem Biotechnol 38(8):3–92Google Scholar
- Rustad T (2003) Utilisation of marine by-products. Electron J Environ Agric Food Chem 2:458–463Google Scholar
- Wang Y, Ma AL, Zhang HZ, Xue BH, Zhao ZJ, Fu FH, Zhou GY (1997) Experimental studies on the antitumor effect of oyster extract. Chin J Mar Drug 16:18–22Google Scholar