Abstract
ABSTRACTPinctada 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.
Highlights
Natural antioxidant peptides have shown unrivalled strong antioxidant capacity and safety given their excellent physical and chemical properties, including thermal stability and solubility, which differ from synthetic antioxidants (Xie, Huang, Xu, & Jin, 2008)
Soybean antioxidant peptides ranging in size from 600 to 1700 Da were obtained by purification, and their sequence structures were explored using mass spectrometry (Chen, Muramoto, & Yamauchi, 1995; Liu et al, 2014)
The antioxidant peptide from P. fucata had good scavenging capacity against free radicals, such as the IC50 of scavenging DPPH and ∙OH of nature antioxidant were closer to vitamina C (Vc) and BHT, the IC50 values of Á OÀ2 of FC2 were a bit poor
Summary
Natural antioxidant peptides have shown unrivalled strong antioxidant capacity and safety given their excellent physical and chemical properties, including thermal stability and solubility, which differ from synthetic antioxidants (Xie, Huang, Xu, & Jin, 2008). Peptide fragments with activity and function could be released from protein chain by specific protease enzymes, whereas the long protein chain does not exhibit these activities. The enzymatic hydrolysate was a mixture, and the antioxidant activity of different peptide fragments varied widely based on the amino acid composition, sequence and structure Recent studies have focused on plant proteins, especially soybean proteins. Soybean antioxidant peptides ranging in size from 600 to 1700 Da were obtained by purification, and their sequence structures were explored using mass spectrometry (Chen, Muramoto, & Yamauchi, 1995; Liu et al, 2014). Numerous antioxidant peptides were purified from milk proteins and aquacultures, and the active sequence was usually different
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