Purification and identification of an antioxidant peptide from Pinctada fucata muscle

Abstract

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 highperformance 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 IC 50 of scavenging 2,2-diphenyl-1picrylhydrazyl and •OH of FC2 were closer to vitamin C and butylated hydroxytoluence; however, the IC 50 values of Á O À 2 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.

Preparation of astaxanthin-loaded liposomes: characterization, storage stability and antioxidant activity

“…The reducing power was determined using the method by Wu et al (2017). About 1.0 mL of 1% potassium ferricyanide (K 3 Fe(CN) 6 ) was added to astaxanthin-LL and astaxanthinliposomes mixture (1.0 mL).…”

“…In this context, recently numerous methods are being dealt to improve the stability, solubility, and bioavailability of astaxanthin. Astaxanthin was incorporated into polymers (Tachaprutinun, Udomsup, Luadthong, & Wanichwecharungruang, 2009), embedded in a blend of egg yolk phosphatidylcholine (EYPC) and cholesterol (Peng, Chang, Peng, & Chyau, 2010), encapsulated by protein-based foods (Anarjan & Tan, 2013), embedded in hydroxypropyl-β-cyclodextrin (Yuan, Du, Jin, & Xu, 2013), encapsulated into a mixture of protein and carbohydrate (Shen & Quek, 2014), and embedded in DNA/chitosan (Wang et al, 2017).…”

Two novel potent ACEI peptides isolated from Pinctada fucata meat hydrolysates using in silico analysis: identification, screening and inhibitory mechanisms

“…[10][11][12] Previous studies have reported that the peptides prepared from P. fucata by a series of traditional methods exhibit several potent bioactivities, such as antioxidant and ACEI activity. For example, Wu et al 13 identied an antioxidant peptide from P. fucata muscle with the sequence GAGLPGKRER, which exhibited strong antioxidant activity close to that of vitamin C and butylated hydroxytoluene. Sasaki et al 12 puried the pearl oyster shell protein hydrolysate using a gel Sephadex G-25 column and high-performance liquid chromatography (HPLC), from which the ACEI hexapeptide GVGSPY was identied, which had an IC 50 value of 5.82 mg mL À1 .…”

Molecular modification, expression and purification of new subtype antioxidant peptide from Pinctada fucata by recombinant Escherichia coli to improve antioxidant-activity

“…For example, the chemical synthesis peptide were obtained using solid phase technologies, based on the sequence which isolated from Pinctada fucata by enzyme hydrolysis in previous study, to clear the relationship between primary structure of the peptide and its antioxidant activity. However, the L-conformation type amino acids were commonly chosen to synthesize peptide in the previous work (Guo et al 2009;Wu et al 2017). So this could make chemosynthesis peptide forming a linear structure according to the identified peptide sequence, and this primary structure could be different compared with natural peptide by enzyme hydrolysis method.…”