Purification and identification of an antioxidant peptide from Pinctada fucata muscle | Purificación e identificación de un péptido antioxidante del músculo de Pinctada fucata
Wu, Yanyan | Wang, Jing | Li, Laihao | Yang, Xianqing | Wang, Jinxu | Hu, Xiao
Pinctada fucata muscles were hydrolysed by alcalase and filtered using ultrafiltration membranes to obtain peptides with molecular weights (MWs) less than 5 kDa. The percolate was then freeze-dried and named crude antioxidant peptides mixture from Pinctada fucata muscles (AOP). In this study, AOP was purified sequentially using sephadex gel chromatography, next reversed-phase high-performance liquid chromatography. The MW of the antioxidant peptide from P. fucata muscle was 1039.56 Da. The amino acid sequence was Gly–Ala–Gly–Leu–Pro–Gly–Lys–Arg–Glu–Arg based on matrix-assisted laser desorption ionization mass spectrometry (MALDI-TOF). The natural peptide exhibits good scavenging capacity against free radicals; the IC₅₀ of scavenging 2,2-diphenyl-1-picrylhydrazyl and ∙OH of FC2 were closer to vitamin C and butylated hydroxytoluence; however, the IC₅₀ values of of FC2 were a bit poor. Its antioxidant activity was attributed to the hydrophobic amino acid residues enriched in the N-terminal and electrophilic ability mediated by Glu and electron acceptors such as Lys and Arg. The synthesized peptide exhibited a reduced ability to scavenge free radicals compared to the natural peptide. The proposed method is a feasible technique to prepare antioxidant peptides from P. fucata and could be useful to obtain ingredients in nutraceutical and cosmetic applications.
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