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The anti-fatigue activities of loach protein hydrolysates with different antioxidant activities
Lijun You , Jiaoyan Ren , Bao Yang , Joe Regenstein , and Mouming Zhao
J. Agric. Food Chem., Just Accepted Manuscript
DOI: 10.1021/jf3037825
Publication Date (Web): November 8, 2012
Copyright © 2012 American Chemical Society

The antioxidant and anti-fatigue activities of two peptides of <5 kD were determined, i.e., loach peptide A (LPA, from a papain digestion) and loach peptide B (LPB, from a flavorenzyme digestion). Their degrees of hydrolysis were 21±0.21% and 35±0.32%, respectively. LPA fraction mainly possessed peptides of 1000<MW<3000 Da (65.41%), while LPB mainly possessed peptides of 500<MW<1000 Da (58.27%). LPA fraction contained 116.3 mg amino acid residues/g loach peptide powder of branched-chain amino acids, 1.42-fold of that in LPB. LPA had stronger in vitro antioxidant activity than LPB. Compared with LPB, LPA increased swimming time more effectively, and reduced blood urea nitrogen (BUN) and liver malonaldehyde (MDA) levels in mice, although both of them had significant anti-fatigue effects compared to the control (P < 0.05). Pearson correlation analysis showed that the anti-fatigue activity of loach peptide was highly correlated with its antioxidant activities.