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Purification, identification, and antioxidative mechanism of three novel selenium-enriched oyster antioxidant peptides
[Display omitted] •The Se-enriched oyster antioxidant peptides were purified by RP-HPLC.•Three novel Se-enriched peptides LLVSeMY, MMDSeML, and VSeMDSeML were obtained.•Se-enriched peptides exhibited excellent cellular antioxidant activity and cytoprotective effect.•The antioxidative mechanism of Se...
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Published in: | Food research international 2022-07, Vol.157, p.111359-111359, Article 111359 |
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Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | [Display omitted]
•The Se-enriched oyster antioxidant peptides were purified by RP-HPLC.•Three novel Se-enriched peptides LLVSeMY, MMDSeML, and VSeMDSeML were obtained.•Se-enriched peptides exhibited excellent cellular antioxidant activity and cytoprotective effect.•The antioxidative mechanism of Se-enriched peptides were predicted using molecular docking.
Natural organic selenium (Se) has multiple physiological health benefits and has become a hotspot of research in recent years. In this study, the Se-enriched antioxidant peptides were purified from Se-enriched oyster hydrolysate. Three novel Se-enriched antioxidant peptides LLVSeMY (685.2953 Da), MMDSeML (687.1875 Da) and VSeMDSeML (703.1599 Da) were identified from fraction F6-4, which all exhibited strong cellular antioxidant activity (CAA) with EC50 values of 0.739, 0.423, and 0.395 μg/mL, respectively. These three Se-enriched antioxidant peptides (0.025 mg/mL) could significantly enhanced cell viability to 84.60 ± 3.32% ∼ 86.18 ± 1.36% compared with the AAPH injury group (75.99 ± 0.79%), and the cytoprotective effects were even better than that of GSH (80.47 ± 2.78%). Moreover, these three Se-enriched peptides also significantly protected HepG2 cells from AAPH-induced oxidative injury by inhibiting ROS production and enhancing the activities of antioxidant enzymes. The molecular docking results showed that these three Se-enriched peptides can form stable hydrogen and hydrophobic bonds with key amino acid residues of Keap1 protein, thereby potentially regulating the Keap1-Nrf2 pathway. In conclusion, the three novel Se-enriched oyster antioxidant peptides are expected to be used in medicine or functional food, providing a new theoretical basis for the high-value utilization of natural organic Se. |
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ISSN: | 0963-9969 1873-7145 |
DOI: | 10.1016/j.foodres.2022.111359 |