The amino acid profile of oyster (Ostrea plicatula Gmelin) peptides (OP) was assayed. Its in vitro antioxidant activity was determined, and its in vivo anti-fatigue activity was compared with those of oyster meat and oyster protein. Seven amino acids that may play an important role in enhancing antioxidant activity account for 25.8% of total OP content. These amino acids are histidine, proline, methionine, cysteine, tyrosine, tryptophan, and phenylalanine. The F-value of OP was 4.89, and the concentration of taurine was 45.43 mmol/mL. OP acted as a scavenger for hydroxyl radicals, 1,1-diphenyl-2-picrylhydrazyl, and superoxide anion radicals. It also inhibited lipid peroxidation. The intragastric administration of OP prolonged the swimming time to exhaustion of mice by 78% over that of the control. It decreased the levels of serum lactic acid and blood urea nitrogen by 24.8% and 11.2%, respectively. Finally, it increased the levels of liver glycogen (1.0-fold) and gastrocnemius muscle glycogen (55.6%).Keywords: oyster peptides, antioxidant activity, anti-fatigue effect, endurance exercise *To whom correspondence should be addressed. E-mail: zhangch2@139.com
IntroductionAcute and/or chronic exercises are associated with increases in free radicals and ROS production, which are due primarily to the increase in oxygen uptake by active tissues (Ji, 1995;Powers and Jackson, 2008). The imbalance between free radical/ROS production and its removal by antioxidant defense systems causes oxidative stress (Chalamaiah et al., 2012). Oxidative stress may lead to potential damage and consequently diminish athletic performance. Thus, increased free radical/ROS production has been associated with altered muscle function and elevated rates of muscle fatigue (Deaton and Marlin, 2003).Research consensus reflects support for the idea that antioxidative peptides can reduce the damage induced by ROS and free radicals. The antioxidative peptides from aquatic products have become of recent concern because they are considered safe and healthy molecules with low molecular weight, easy absorption, low cost, and high activity (Sarmadi and Ismail, 2010). The precursor protein in these peptides is mostly inactive. These active peptides can also be released from the precursor protein by hydrolysis techniques, such as enzymatic hydrolysis, autolytic process using endogenous enzymes, and microbial fermentation (Chalamaiah et al., 2012;Je et al., 2007;Rajapakse et al., 2005;Kim et al., 2007).In this study, we assayed the amino acid profile of oyster peptides (OP), and then investigated its in vitro antioxidant activities and the in vivo anti-fatigue effects of OP previously prepared by neutral proteinase digestion. The in vitro antioxidant activities were studied by determining the activities of hydroxyl radicals, 1,1-diphenyl-2-picrylhydrazyl (DPPH), and superoxide anion radical scavengers, as well as lipid peroxidation inhibitory activity in a linoleic acid emulsion system. In the determination, glutathione (GSH) which is a well known peptide an...