Abstract:Mackerel (Pneumatophorus japonicus) viscera contain large amount of protein. We used five proteases to hydrolyze the viscera, and the hydrolysate treated by neutrase exhibited the highest nitrogen recovery (NR). Then we optimized the preparation conditions for mackerel viscera hydrolysate (MVH) by response surface methodology and investigated the antioxidant activity of MVH. The optimal conditions were as follows: enzyme concentration of 1,762.87 U/g, pH of 6.76, temperature of 43.75 °C, extraction time of 6.0… Show more
“…Additionally, the cellular antioxidant activity initially increased and then decreased slightly as the X 4 increased from 1 to 9, as shown in Figure 3H,J. We speculated that a higher X 4 may dilute the X 1 and slow the rate of enzyme reactions [22].…”
The aim of this study was to isolate and purify antioxidative peptides from Pacific herring (Clupea pallasii) protein. Five enzymes (pepsin, trypsin, papain, flavourzyme, and neutrase) were used for protein hydrolysis, and Pacific herring protein hydrolysates (PHPH) were separated by ultrafiltration. The fraction with the molecular weight below 3500 Da exhibited the highest in vitro antioxidant activities and cellular antioxidant activity. The PHPH was isolated and purified by consecutive chromatographic methods including gel filtration chromatography and reverse high-performance liquid chromatography (RP-HPLC). The purified antioxidant peptides were identified as Leu-His-Asp-Glu-Leu-Thr (MW = 726.35 Da) and Lys-Glu-Glu-Lys-Phe-Glu (MW = 808.40 Da), and the IC50 values of cellular antioxidant activity were 1.19 ± 0.05 mg/mL and 1.04 ± 0.06 mg/mL. The results demonstrate that is possible to produce natural antioxidative peptides from Pacific herring protein via enzymatic hydrolysis and purification.
“…Additionally, the cellular antioxidant activity initially increased and then decreased slightly as the X 4 increased from 1 to 9, as shown in Figure 3H,J. We speculated that a higher X 4 may dilute the X 1 and slow the rate of enzyme reactions [22].…”
The aim of this study was to isolate and purify antioxidative peptides from Pacific herring (Clupea pallasii) protein. Five enzymes (pepsin, trypsin, papain, flavourzyme, and neutrase) were used for protein hydrolysis, and Pacific herring protein hydrolysates (PHPH) were separated by ultrafiltration. The fraction with the molecular weight below 3500 Da exhibited the highest in vitro antioxidant activities and cellular antioxidant activity. The PHPH was isolated and purified by consecutive chromatographic methods including gel filtration chromatography and reverse high-performance liquid chromatography (RP-HPLC). The purified antioxidant peptides were identified as Leu-His-Asp-Glu-Leu-Thr (MW = 726.35 Da) and Lys-Glu-Glu-Lys-Phe-Glu (MW = 808.40 Da), and the IC50 values of cellular antioxidant activity were 1.19 ± 0.05 mg/mL and 1.04 ± 0.06 mg/mL. The results demonstrate that is possible to produce natural antioxidative peptides from Pacific herring protein via enzymatic hydrolysis and purification.
“…Based on the above data, different response values were obtained for hydrolysates generated with different independent variable conditions. In our DH assay study, the DH content of the OP increased significantly when the hydrolysis time increased from 5.0 h to 6.0 h and decreased significantly with a hydrolysis time from 6.0 h to 7.0 h. This trend was consistent with the results of Wang et al [ 12 ], which showed that the DH of fish gelatin hydrolysate increased significantly ( p < 0.05) when the time increased from 1.0 h to 2.0 h, and decreased slowly when the time increased from 2.0 h to 3.0 h. We inferred that the hydrolysis reaction was powerful in the first few hours because of the sufficient raw material and enzyme quantity, and the reaction flattened later with the consumption of raw material and protease [ 19 ]. Some studies have come to different conclusions; for example, Zheng et al [ 20 ] found that the DH value obtained from alcalase increased rapidly during the first 2.0 h of the reaction and then slowly increased, while the hydrolysates obtained from bromelain achieved an obvious increase after 2.0 h. Tan et al [ 21 ] found that the DH of cod bone protein increased rapidly during the first 0.5 h because more peptide bonds were broken, and then the DH showed a slow increase.…”
Oyster (Crassostrea talienwhanensis) protein was hydrolyzed by trypsin to produce peptides with different response values, and response surface methodology (RSM) was applied to optimize the hydrolysis conditions. The highest degree of hydrolysis (DH) of the oyster peptide (OP) was obtained at an enzyme concentration of 1593.2 U/g, a pH of 8.2, a hydrolysis temperature of 40.1 °C, a hydrolysis time of 6.0 h, and a water/material ratio of 8.2. The greatest hydroxyl-radical-scavenging activity of OP was obtained at an enzyme concentration of 1546.3 U/g, a pH of 9.0, a hydrolysis temperature of 50.2 °C, a hydrolysis time of 5.1 h, and a water/material ratio of 5.6. The largest branched-chain amino acid (BCAA) content of OP was obtained at an enzyme concentration of 1323.8 U/g, a pH of 8.3, a hydrolysis temperature of 41.7 °C, a hydrolysis time of 6.7 h, and a water/material ratio of 4.8. The three experimental values were significantly in agreement with the predicted values within the 95% confidence interval. Furthermore, ultrafiltration and chromatographic methods were used to purify the OP, and 13 peptides that were rich in Lys, Arg, His, and Thr were identified by LC-MS/MS. The results of this study offer different optimum hydrolysis conditions to produce target peptides from oyster protein by using RSM, and this study provide a theoretical basis for the high-value utilization of oyster protein.
“…The DPPH scavenging activity was assessed following the method described by Paul et al [ 29 ]. Briefly, a mixture of 1 mL JPHT-2 solution and 1 mL DPPH solution (0.1 mM in ethanol) was prepared and incubated at room temperature for 30 min in the absence of light.…”
Jellyfish is a valuable biological resource in marine ecosystems, and blooms been observed in numerous coastal regions. However, their utility is limited by their high water content. Recent research has focused on extracting antioxidants from marine sources. In this study, we obtained jellyfish peptides (JPHT-2) through enzymatic hydrolysis of lyophilized jellyfish powder under optimal conditions and measured their antioxidant activity. Our findings indicate that JPHT-2 possesses significant radical-scavenging activity and reducing power. At a concentration of 0.74 mg/mL, JPHT-2 exhibited a remarkable ability to scavenge hydroxyl radicals, with a rate of up to 50%. The EC50 values for scavenging superoxide anion and DPPH radical were 1.55 mg/mL and 1.99 mg/mL, respectively. At the cellular level, JPHT-2 was able to protect HaCaT cells from H2O2-induced oxidative damage by increasing the level of superoxide dismutase (SOD) in cells. In conclusion, jellyfish peptides with low molecular weight can be easily obtained through hydrolysis with three enzymes and exhibit excellent antioxidant activity and safety. Jellyfish can serve as a promising source of antioxidants.
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