Purification and characterization of antioxidant peptides from hairtail surimi hydrolysates and their effects on beef color stability

Abstract

The antioxidant peptides extracted from plants or animals have shown great potential in preventing food quality deterioration caused by oxidization. Here, peptide fractions obtained from hairtail surimi hydrolysates (HSH) were investigated for structure and color‐protective effect. The results showed the <3 kDa fraction obtained from HSH by ultrafiltration could be separated into five major fractions (A–E) by gel chromatography, among which fraction A possessed the highest antioxidant activities. This fraction A could be further separated into two fractions (A1 and A2) by the reversed‐phase high‐performance liquid chromatography, and fraction A2 with lower α‐helix content exhibited the higher antioxidant activities. The amino acids sequence of fraction A2 was identified as DLYANTVLSGGTTMYPGIADR (2214.0627 Da). The synthetic peptide with this sequence was also found to exhibit obvious antioxidant activity. Moreover, both HSH, fractions A1 and A2, and synthetic peptide demonstrated color‐protective effects during the beef preservation. Taken together, the results obtained showed that the natural antioxidant peptides could be isolated from HSH, which can be used in meat preservation for inhibiting color deterioration. Practical Application This study demonstrated the potential of hairtail surimi hydrolysates (HSH) as a source of antioxidant peptides. Furthermore, these antioxidant peptides purified from HSH exhibited the potential for prevention of beef color deterioration of beef, providing a potential application for meat preservation. Particularly, using the antioxidant peptides sourced from fish surimi for meat preservation may not only ease the safety concerns about artificial preservatives but also create a unique selling proposition, especially in far eastern Asian countries, since consumers in these countries believe “umami” is the combination of “fish” and “meat.”

Physiological and Clinical Aspects of Bioactive Peptides from Marine Animals

“…The sturgeon peptide, GDRGESGPA (845.37 Da), having glycine and alanine, showed DPPH • scavenging activity of 40% [101]. Hairtail surimi peptide, DLYANTVLSGGTTMYPGIADR (2.2 kDa), having leucine, glycine, isoleucine, and alanine, showed DPPH • and • OH scavenging activity of 67.07% and 62.08%, respectively [100]. Furthermore, oyster peptide, LANAK (515.29 Da), showing DPPH • scavenging activity of 83.79%, also contained leucine and alanine [87].…”

Cryoprotective effect of glycopeptide complex from abalone viscera on frozen surimi and its underlying mechanism

“…During freezing storage, the protein of surimi will undergo freezing denaturation, and the activity of endogenous protease will decrease (Zhang et al., 2020a), resulting in loss of emulsification, gel, and other important functional properties (Nikoo et al., 2016). In addition to the denaturation of surimi and its proteins caused by low‐temperature storage, oxidation is another reason for protein denaturation of surimi, and protein oxidation still exists in the process of freezing storage (Wang et al., 2021). Some studies have reported the mechanism of protein oxidation in surimi products, which can be summarized as a free radical chain reaction directly triggered by reactive oxygen species and active nitrogen or indirectly triggered by secondary products produced by oxidation (Soladoye et al., 2015).…”