Details
| Original language | English |
|---|---|
| Pages (from-to) | 231-243 |
| Number of pages | 13 |
| Journal | International Journal of Peptide Research and Therapeutics |
| Volume | 20 |
| Issue number | 2 |
| Publication status | Published - 19 Dec 2013 |
Abstract
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.
Keywords
- Antioxidant peptide, DPPH, Electrospray ionization mass spectrometry, Enzymatic hydrolysis, Oyster Saccostrea cucullata, Protein hydrolysate
ASJC Scopus subject areas
- Chemistry(all)
- Analytical Chemistry
- Chemical Engineering(all)
- Bioengineering
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Medicine
- Pharmacology, Toxicology and Pharmaceutics(all)
- Drug Discovery
Sustainable Development Goals
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In: International Journal of Peptide Research and Therapeutics, Vol. 20, No. 2, 19.12.2013, p. 231-243.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Purification and characterization of antioxidant peptides from oyster (Saccostrea cucullata) hydrolysate and the anticancer activity of hydrolysate on human colon cancer cell lines
AU - Umayaparvathi, S.
AU - Arumugam, M.
AU - Meenakshi, S.
AU - Dräger, Gerald
AU - Kirschning, Andreas
AU - Balasubramanian, T.
N1 - Funding information: Acknowledgments 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 An-namalai University for providing the necessary facilities.
PY - 2013/12/19
Y1 - 2013/12/19
N2 - 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.
AB - 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.
KW - Antioxidant peptide
KW - DPPH
KW - Electrospray ionization mass spectrometry
KW - Enzymatic hydrolysis
KW - Oyster Saccostrea cucullata
KW - Protein hydrolysate
UR - http://www.scopus.com/inward/record.url?scp=84899064594&partnerID=8YFLogxK
U2 - 10.1007/s10989-013-9385-5
DO - 10.1007/s10989-013-9385-5
M3 - Article
AN - SCOPUS:84899064594
VL - 20
SP - 231
EP - 243
JO - International Journal of Peptide Research and Therapeutics
JF - International Journal of Peptide Research and Therapeutics
SN - 1573-3149
IS - 2
ER -