In this study, the anti-fatigue effect and mechanism of Auxis thazard oligopeptide (ATO) were studied by exhaustive swimming in mice. The results showed that ATO could significantly prolong the exhaustive...
Auxis thazard meat was hydrolyzed by alkaline protease. Auxis thazard hydrolysate (ATH) obtained was isolated by ultrafiltration, size exclusion chromatography and reversed-phase high-performance liquid chromatography. Two peptides with high XOD inhibitory activity purified from ATH were identified as Pro-Asp-Leu (PDL, 344.87 Da) and Ser-Val-Gly-Gly-Ala-Leu (SVGGAL, 504.26 Da) by UPLC-MS/MS, which possessed high in vitro XOD inhibitory activity with the IC 50 values of 4.37 ± 0.11 mg mL -1 and 5.59 ± 0.09 mg mL -1 , respectively. Molecular simulation indicated that PDL and SVGGAL binded to XOD mainly through hydrogen bond and hydrophobic interaction, thereby inhibiting XOD activity. The research results suggested that the two peptides had potential application prospects as a safe XOD inhibitor substance for hyperuricemia treatment.
In order to promote the development and application of small molecule oligopeptides from tilapia (SMOT), its anti-fatigue effect was evaluated by using exhaustive swimming in mice. The results showed that compared with the negative control group, SMOT could significantly prolong the exhausted swimming time of mice, reduce blood lactic acid, blood urea nitrogen and malondialdehyde content, and could significantly improve liver glycogen storage status. Meanwhile, the activities of superoxide dismutase and glutathione peroxidase of the mice gavaged with SMOT were significantly higher than those in the negative control group. In addition, SMOT could increase the activity of immune factor IL-2, stimulate the secretion of sIgA and regulate the level of inflammatory factors. So SMOT had significant anti-fatigue effect. Its anti-fatigue effect was exerted by increasing energy reserves, eliminating the accumulation of metabolites, reducing oxidative stress, and improving the body's immune function.
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