Effects of fermentation periods on antioxidant and angiotensin I-converting enzyme inhibitory activities of peptides from fish sauce by-products

Khositanon, Petlada; Panya, Naphatsawan; Roytrakul, Sittiruk; Krobthong, Sucheewin; Chanroj, Salil; Choksawangkarn, Waeowalee

doi:10.1016/j.lwt.2020.110122

Cited by 19 publications

(20 citation statements)

References 28 publications

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“…DPPH radical scavenging activity was analyzed as previously described [26,36] with slight modifications. A 0.1 mL of JPH was mixed with 1.9 mL of 0.15 mmol/L DPPH in 70% ethanol.…”

Section: Antioxidant Activity (Dpph Radical Scavenging Assay)mentioning

confidence: 99%

“…Antioxidant activity, the ability to reduce or scavenge free radicals, is one of the major biological activities of protein hydrolysates that have mostly been reported [3]. If the number of free radicals exceeds normal, free radicals can cause diseases such as arthritis, diabetes, atherosclerosis, ageing, and cancer [8,26]. Then, the novel protein sources of bioactive peptides having antioxidant activities are currently of interest for reducing the risk of various diseases [26].…”

Section: Introductionmentioning

confidence: 99%

“…If the number of free radicals exceeds normal, free radicals can cause diseases such as arthritis, diabetes, atherosclerosis, ageing, and cancer [8,26]. Then, the novel protein sources of bioactive peptides having antioxidant activities are currently of interest for reducing the risk of various diseases [26]. The marine source has become attractive with various organisms that have potentially been reported for biological activities.…”

Section: Introductionmentioning

confidence: 99%

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Effect of pepsin hydrolysis on antioxidant activity of jellyfish protein hydrolysate

et al. 2021

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Edible jellyfish have been consumed as food for more than a century with offering high protein and crunchy texture. The pepsin hydrolysis of jellyfish protein yields jellyfish protein hydrolysate (ep-JPH), reported for potential bioactivities such as antioxidant activity or antihypertensive activities. Due to the substantial number of by-products generated from jellyfish processing, the by-products were then selected as a raw material of JPH production. This research aimed to evaluate the effect of the hydrolysis time of pepsin on the antioxidant activity of ep-JPH. The dried desalted jellyfish by-products powder was enzymatically hydrolysed by 5% (w/w) pepsin, and the hydrolysis time was varied from 6, 12, 18, and 24 h at 37oC. Results showed that increased hydrolysis time increased the degree of hydrolysis (DH) and inhibition of DPPH radical. The 24 h ep-JPH possessed the highest DH and the highest inhibitory effect of DPPH radical. The results demonstrated that, in this experiment, all ep-JPHs were DPPH radical scavengers, exhibiting different inhibition activities depending on DH values.

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“…DPPH radical scavenging activity was analyzed as previously described [26,36] with slight modifications. A 0.1 mL of JPH was mixed with 1.9 mL of 0.15 mmol/L DPPH in 70% ethanol.…”

Section: Antioxidant Activity (Dpph Radical Scavenging Assay)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Effect of pepsin hydrolysis on antioxidant activity of jellyfish protein hydrolysate

et al. 2021

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“…Peptides produced from various fish proteins have been shown to behave as potential antioxidants with various modalities of antioxidant activity, including electron/hydrogen atom donation, scavenging of reactive oxygen species (ROS)/free radicals, and sequestration of pro-oxidants [10][11][12][13][14][15]. One of the most significant antioxidant mechanisms in biological systems is the removal of ROS and other free radicals [16].…”

Section: Introductionmentioning

confidence: 99%

Characterization of Antioxidant Peptides from Thai Traditional Semi-Dried Fermented Catfish

et al. 2021

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Herein, the antioxidant peptides from a Thai traditional semi-dried fermented farmed hybrid catfish (Clarias macrocephalus × Clarias gariepinus) catfish, Pla Duk Ra, were characterized. After extraction and deproteinization, Pla Duk Ra crude peptide extract (CPE) was fractioned using 2 connected Hitrap Sephadex-G25 columns, yielding two significant fractions, F1 with higher browning intensity (A420) and F2. CPE, F1, and F2 had different amino acid profiles, contents, and sequences evaluated by LC-MS/MS, which could be responsible for their antioxidant properties. F2 contained the highest numbers of hydrophobic amino acid (HBA) (47.45%) and aromatic amino acid (27.31%), followed by F1, and CPE. The peptides with 8–24 amino acid residues were detected in CPE and its fractions. In CPE, F1, and F2, there were 69, 68, and 85 peptides with varied HBA content, respectively. ARHSYGMLYCSCPPND (50% HBA), ALRKMGRK (37.5% HBA), and ANWMIPLM (87.5% HBA) were the most prevalent peptides found in CPE, F1, and F2. Overall, F2 was the most effective at inhibiting free radicals (DPPH● and ABTS●+) and reactive oxygen species (hydroxyl radical, singlet oxygen, and hydrogen peroxide), followed by F1 and CPE. The metal chelation of F1 was, however, superior to that of F2 and CPE. For the stability test, the effects of pH, heating temperature, and in vitro digestion on the DPPH● scavenging activity of F2 were investigated. The activity was boosted by lowering the pH and raising the heating temperature. In the gastrointestinal tract model system, however, roughly 50% of DPPH● scavenging activity reduced after digesting.

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“…Nonetheless, the antioxidant activities of the peptides were lower than that of positive control. Peptides with molecular weight < 3 kDa were associated with higher antioxidant activities [ 45 ]. However, this was not observed in our results, as the molecular weight of MIPs and DIPs ranged between 0.5 and 2.0 kDa.…”

Section: Resultsmentioning

confidence: 99%

Multifunctional Tyrosinase Inhibitor Peptides with Copper Chelating, UV-Absorption and Antioxidant Activities: Kinetic and Docking Studies

Yap

Gan

2021

Foods

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Nature-derived tyrosinase inhibitors are of great industrial interest. Three monophenolase inhibitor peptides (MIPs) and three diphenolase inhibitor peptides (DIPs) from a previous study were investigated for their in vitro tyrosinase inhibitory effects, mode of inhibition, copper-chelating activity, sun protection factor (SPF) and antioxidant activities. DIP1 was found to be the most potent tyrosinase inhibitor (IC50 = 3.04 ± 0.39 mM), which could be due to the binding interactions between its aromatic amino acid residues (Y2 and D7) with tyrosinase hotspots (H85, V248, H258, H263, F264, R268, V283 and E322) and its ability to chelate copper ion within the substrate-binding pocket. The conjugated planar rings of tyrosine and tryptophan may interact with histidine within the active site to provide stability upon enzyme-peptide binding. This postulation was later confirmed as the Lineweaver–Burk analysis had identified DIP1 as a competitive inhibitor and DIP1 also showed 36.27 ± 1.17% of copper chelating activity. In addition, DIP1 provided the highest SPF value (11.9 ± 0.04) as well as ferric reducing antioxidant power (FRAP) (5.09 ± 0.13 mM FeSO4), 2,2′–azinobis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) (11.34 ± 0.90%) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) (29.14 ± 1.36%) free radical scavenging activities compared to other peptides. These results demonstrated that DIP1 could be a multifunctional anti-tyrosinase agent with pharmaceutical and cosmeceutical applications.

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Effects of fermentation periods on antioxidant and angiotensin I-converting enzyme inhibitory activities of peptides from fish sauce by-products

Cited by 19 publications

References 28 publications

Effect of pepsin hydrolysis on antioxidant activity of jellyfish protein hydrolysate

Effect of pepsin hydrolysis on antioxidant activity of jellyfish protein hydrolysate

Characterization of Antioxidant Peptides from Thai Traditional Semi-Dried Fermented Catfish

Multifunctional Tyrosinase Inhibitor Peptides with Copper Chelating, UV-Absorption and Antioxidant Activities: Kinetic and Docking Studies

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