Abstract:In this study, antioxidant peptides were prepared from hairtail surimi by hydrolysis. Response surface methodology coupled with a Box-Behnken design was applied to optimize hydrolysis conditions. The optimum conditions were determined as: 12.1 h incubation time, 44.74 °C incubation temperature and enzyme concentration 1858.85 U/g. The amino acid compositions analysis showed most abundant amino acid in hairtail surimi antioxidant peptides (HAP) was Glutamic acid followed by Aspartic acid and Lysine. In addition… Show more
“…Enzymatic hydrolysis is an important method to explore the added value of hairtail proteins (Cotabarren et al., 2019). In our previous study, the low molecular peptides (<3 kDa) isolated from HSH exhibited good antioxidant activities, making it a promising candidate for exploring natural antioxidants for meat preservation (Wang, Lin, et al., 2020). Thus, in the current study, the <3 kDa fraction of HSH was further purified using gel filtration chromatography into five fractions (A–E) on a Sephadex G‐15 column.…”
Section: Resultsmentioning
confidence: 99%
“…Our previous research already showed that hairtail surimi hydrolysates (HSH) exhibited beneficial effects in scavenging free radicals (Wang, Lin, et al., 2020). Particularly, the peptide fraction with molecular weight less than 3 kDa purified by ultrafiltration showed the stronger antioxidant activity than all the other fractions (3–5 kDa, 5–10 kDa, and > 10 kDa peptide fractions).…”
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.”
“…Enzymatic hydrolysis is an important method to explore the added value of hairtail proteins (Cotabarren et al., 2019). In our previous study, the low molecular peptides (<3 kDa) isolated from HSH exhibited good antioxidant activities, making it a promising candidate for exploring natural antioxidants for meat preservation (Wang, Lin, et al., 2020). Thus, in the current study, the <3 kDa fraction of HSH was further purified using gel filtration chromatography into five fractions (A–E) on a Sephadex G‐15 column.…”
Section: Resultsmentioning
confidence: 99%
“…Our previous research already showed that hairtail surimi hydrolysates (HSH) exhibited beneficial effects in scavenging free radicals (Wang, Lin, et al., 2020). Particularly, the peptide fraction with molecular weight less than 3 kDa purified by ultrafiltration showed the stronger antioxidant activity than all the other fractions (3–5 kDa, 5–10 kDa, and > 10 kDa peptide fractions).…”
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.”
“…The binding of protein hydrolysates to metal ions results in antioxidant effects (Wang, et al, 2020) since the peptides present in these hydrolysates bind to the transition metals that stop promoting oxidative damage, cell degeneration, breakage or oxidation of nucleic acids (Kurutas, 2016;Liu, et al, 2020).…”
In the present study, buffalo milk caseinate hydrolysates produced by bromelain, neutrase, papain and trypsin were ultra-filtered and different fractions were assessed for antioxidant, inhibition of angiotensin converting enzyme and antimicrobial activity. Biological potential was assessed by a number of metrics: ability to remove radicals of 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid), 2,2'-diphenyl-1-picrylhydrazyl (DPPH) and hydroxyls; copper and iron chelation; antidiabetic properties; antihypertensive assay; and antibacterial activity against Escherichia coli ATCC 25922, Listeria monocytogenes ATCC 19114, Salmonella typhimurium ATCC 14028 and Staphylococcus aureus ATCC 25923 strains. The tests for scavenging of hydroxyl radicals and DPPH revealed a greater potential in the 3–10 kDa fractions. Iron chelation activity >70% was observed in all the fractions, including <3 kDa. Copper chelation was >60% in fractions >10 kDa. α-Amylase inhibition and antihypertensive activity was optimal in the <3 kDa fraction. Antibacterial activity ranged between 3.28 and 100% inhibition against microorganisms tested, the fraction <3 kDa showed a greater inhibitory potential. The antihypertensive activity of fractions ranged between 39.35 and 89.58%. All treatments were able to produce hydrolysates and fractions with biological potential and, so the ultrafiltration method proved to be effective in the separation of peptides with different molar masses and potential use in the food or pharmaceutical industry.
“…This may be due to the destruction of the specific peptide structure and amino acid side chain resulting in protein denaturation. 84 In addition, the presence of a high concentration of salt will reduce the solubility of antioxidant peptides, thus reducing the activity. 92 The stability of antioxidant peptides also depends upon the type of salt involved.…”
Section: ■ Factors Affecting the Stability Of Bioactive Peptides In F...mentioning
Bioactive peptides used for food preservation can prolong the shelf life through bacteriostasis and antioxidation. On the one hand, bioactive peptides can inhibit lipid oxidation by scavenging free radicals, interacting with metal ions, and inhibiting lipid peroxidation. On the other hand, bioactive peptides can fundamentally inhibit the growth and reproduction of microorganisms by destroying their cell membranes or targeting intracellular components. Besides, bioactive peptides are biocompatible and biodegradable in vivo. Therefore, they are regarded as a promising alternative to chemical preservatives. However, bioactive peptides are easily affected by the external environment in practical application, which hinders their commercialization. Currently, the studies to overcome the weakness focus on encapsulation and chemical synthesis. Bioactive peptides have been applied to the preservation of various foods in experimental research, with good results. In the future, with the deepening understanding of their safety and structure−activity relationship, there may be more bioactive peptides as food preservatives.
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