Identification and characterization of antioxidant peptides from hydrolysate of blue-spotted stingray and their stability against thermal, pH and simulated gastrointestinal digestion treatments

Wong, Fai-Chu; Xiao, Jianbo; Ong, Michelle G-Ling; Pang, Mei-Jing; Wong, Shao-Jun; Teh, Lai Kuan; Chai, Tsun-Thai

doi:10.1016/j.foodchem.2018.07.206

Cited by 93 publications

(85 citation statements)

References 39 publications

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“…Generally, there was no statistically significant difference between the different temperature treatments ( Figure 3B-3E). Our finding is in accordance with the observation of heat-stable ABTS •+ scavenging activity in Nile tilapia protein hydrolysate [32], semen cassiae protein hydrolysate [23], mung bean meal-derived antioxidant peptides [44] and blue-spotted stingray-derived peptides [24]. In this study, a temperature-dependent decrease in the inhibition of lipid peroxidation, as assessed by using the lecithin liposome model, was detected ( Figure 3F).…”

Section: As Shown Insupporting

confidence: 92%

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Trypsin‐hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects

Chai

Ang

Goh

et al. 2020

eFood

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Hematoprotection lipid peroxidation protein hydrolysate simulated gastrointestinal digestion stigma maydis thermal stability A B S T R A C TThe aim of this study was to examine the antioxidant capacity of Trypsin-hydrolyzed corn silk proteins, specifically radical scavenging, ferric reducing and anti-lipid peroxidation activities, as well as stability after heating and simulated gastrointestinal digestion. Among the 1-5-h hydrolysates, the 1-h Trypsin hydrolysate (T1H) was the strongest. T1H exhibited stronger H 2 O 2 [half maximal effective concentration (EC 50 ) = 156.44 µg/mL] and superoxide (EC 50 = 0.33 mg/mL) scavenging activities than glutathione, carnosine and N-acetylcysteine. Radical scavenging activities of T1H were heat-stable (25-100°C), although lost by 20-58% after gastrointestinal digestion. Ferric reducing activity of T1H was heat-stable, even enhanced by 20% after gastrointestinal digestion. Lecithin liposome assay found anti-lipid peroxidation activity of T1H resistant to gastrointestinal peptidases. By contrast, 100°C incubation reduced anti-lipid peroxidation activity of 0.5 mg/mL T1H to 3.5-fold lower than that of 25°C incubation. At 30 µg/mL, T1H (3% hemolysis) was stronger than glutathione (32% hemolysis) in protecting human red blood cells. T1H was 1.5-fold more potent than glutathione and carnosine in alleviating lipid peroxidation in the cells. Overall, T1H demonstrated strong, heat-stable radical scavenging activities, besides partial resistance to gastrointestinal peptidases. T1H was also hematoprotective. T1H is a promising antioxidant for the development of functional food ingredients and nutraceuticals.

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Section: As Shown Insupporting

confidence: 92%

“…and Ferric Reducing Activities 2,2¢-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) radical cation (ABTS •+ ) scavenging activity was determined as described by Wong et al [24], with modifications. Briefly, 20 µL of sample was mixed with 200 µL of ABTS working solution.…”

Section: Determination Of Radical Scavengingmentioning

confidence: 99%

Trypsin‐hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects

Chai

Ang

Goh

et al. 2020

eFood

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“…Although the ability of protein hydrolyzates and bioactive peptides to act as antioxidative agents has been roundly demonstrated during in vitro (Agrawal, Joshi, & Gupta, ; Alashi et al, ; Harnedy et al, ; Lin et al, ; Rahman et al, ; Wong et al, ) and in vivo (Girgih, Alashi et al, ; Liu et al, ; Mada et al, ; Xu, Li et al, ; Zhao et al, ) tests, there is a dearth of human clinical trials replicating the results. Given the challenge often encountered in translating results from animal and chemical‐based assays to clinical outcomes, future work should be designed to include tests in human subjects.…”

Section: Future Research Needsmentioning

confidence: 99%

Structural and functional properties of food protein-derived antioxidant peptides

2019

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The aim of this work is to provide a timely examination of the structure-activity relationship of antioxidative peptides. The main production approach involves enzymatic hydrolysis of animal and plant proteins to produce protein hydrolyzates, which can be further processed by membrane ultrafiltration into size-based peptide fractions. The hydrolyzates and peptide fractions can also be subjected to separation by column chromatography to obtain pure peptides. Although the structural basis for enhanced antioxidant activity varies, protein hydrolyzates and peptide fractions that contain largely low molecular weight peptides have generally been shown to be potent antioxidants. In addition to having hydrophobic amino acids such as Leu or Val in their N-terminal regions, protein hydrolyzates, and peptides containing the nucleophilic sulfur-containing amino acid residues (Cys and Met), aromatic amino acid residues (Phe, Trp, and Tyr) and/or the imidazole ring-containing His have been generally found to possess strong antioxidant properties. Practical applicationsHigh levels of reactive oxygen species (ROS) in addition to the presence of metal cations can lead to oxidative stress, which promotes reactions that cause destruction of critical cellular biopolymers, such as proteins, lipids, and nucleic acids. Oxidative stress could be due to insufficient levels of natural cellular antioxidants, which enables accumulation of ROS to toxic levels. A proposed approach to ameliorating oxidative stress is the provision of exogenous peptides that can be consumed to complement cellular antioxidants. Food protein-derived peptides consist of amino acids joined by peptides bonds just like glutathione, a very powerful natural cellular antioxidant. Therefore, this review provides a timely summary of the in vitro and in vivo reactions impacted by antioxidant peptides and the postulated mechanisms of action, which could aid development of potent antioxidant agents. The review also serves as a resource material for identifying novel antioxidant peptide sources for the formulation of functional foods and nutraceuticals. K E Y W O R D S antioxidants, FRAP, lipid peroxidation, metal chelation, peptides, protein hydrolyzates, radical scavenging [Correction added on 30 January 2019: this article has been added to the issue after an inadvertent omission.]

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“…Figure 3B indicated that DPPH• and HO• scavenging activities of MUA-4-B were 86.39% ± 4.32% and 80.56% ± 3.55% at the concentration of 5.0 mg protein/mL, which were significantly higher than those of MUA-4 (DPPH• 76.64% ± 3.43%; HO• 69.39% ± 3.58%) and MUA-4-A (DPPH• 56.38% ± 3.62%; HO• 55.26% ± 4.39%) (p < 0.05). Gel filtration chromatography is a frequently-used prepared technique according to the MW of the separated substances and is applied to separate peptides from protein hydrolysates and their fractions, such as Spanish mackerel [30], miiuy croaker [10,20], ark shell [19], and blue-spotted stingray [22]. Therefore, fraction MUA-4-B was selected for the following isolation process.…”

Section: Gel Filtration Chromatography Of Mua-4mentioning

confidence: 99%

“…PIIVYWK and FSVVPSPK from Mytilus edulis hydrolysates exhibited strong 2,2-diphenyl-1-picrylhydrazyl radical (DPPH•) scavenging and ORAC activities, and increased cell viabilities in H 2 O 2 -induced hepatotoxicity through upregulating heme oxygenase-1 (HO-1) level under normal and oxidative stress conditions in cultured hepatocytes [21]. WAFAPA and MYPGLA from hydrolysate of blue-spotted stingray surpassed carnosine in their abilities to suppress H 2 O 2 -induced lipid oxidation and protected plasmid DNA and proteins from Fenton's reagent-induced oxidative damage [22]. Therefore, marine proteins are high-quality raw materials for the preparation of APs with the ability to enhance health by reducing oxidative stress.…”

Section: Introductionmentioning

confidence: 99%

Antioxidant Peptides from the Protein Hydrolysate of Monkfish (Lophius litulon) Muscle: Purification, Identification, and Cytoprotective Function on HepG2 Cells Damage by H2O2

Wang

Zhao

et al. 2020

Marine Drugs

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In the work, defatted muscle proteins of monkfish (Lophius litulon) were separately hydrolyzed by pepsin, trypsin, and in vitro gastrointestinal (GI) digestion methods, and antioxidant peptides were isolated from proteins hydrolysate of monkfish muscle using ultrafiltration and chromatography processes. The antioxidant activities of isolated peptides were evaluated using radical scavenging and lipid peroxidation assays and H2O2-induced model of HepG2 cells. In which, the cell viability, reactive oxygen species (ROS) content, and antioxidant enzymes and malondialdehyde (MDA) levels were measured for evaluating the protective extent on HepG2 cells damaged by H2O2. The results indicated that the hydrolysate (MPTH) prepared using in vitro GI digestion method showed the highest degree of hydrolysis (27.24 ± 1.57%) and scavenging activity on a 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (44.54 ± 3.12%) and hydroxyl radical (41.32 ± 2.73%) at the concentration of 5 mg protein/mL among the three hydrolysates. Subsequently, thirteen antioxidant peptides (MMP-1 to MMP-13) were isolated from MPTH. According to their DPPH radical and hydroxyl radical scavenging activity, three peptides with the highest antioxidant activity were selected and identified as EDIVCW (MMP-4), MEPVW (MMP-7), and YWDAW (MMP-12) with molecular weights of 763.82, 660.75, and 739.75 Da, respectively. EDIVCW, MEPVW, and YWDAW showed high scavenging activities on DPPH radical (EC50 0.39, 0.62, and 0.51 mg/mL, respectively), hydroxyl radical (EC50 0.61, 0.38, and 0.32 mg/mL, respectively), and superoxide anion radical (EC50 0.76, 0.94, 0.48 mg/mL, respectively). EDIVCW and YWDAW showed equivalent inhibiting ability on lipid peroxidation with glutathione in the linoleic acid model system. Moreover, EDIVCW, MEPVW, and YWDAW had no cytotoxicity to HepG2 cells at the concentration of 100.0 µM and could concentration-dependently protect HepG2 cells from H2O2-induced oxidative damage through decreasing the levels of reactive oxygen species (ROS) and MDA and activating intracellular antioxidant enzymes of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px). These present results indicated that the protein hydrolysate and isolated antioxidant peptides from monkfish muscle, especially YWDAW could serve as powerful antioxidants applied in the treatment of some liver diseases and healthcare products associated with oxidative stress.

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Identification and characterization of antioxidant peptides from hydrolysate of blue-spotted stingray and their stability against thermal, pH and simulated gastrointestinal digestion treatments

Cited by 93 publications

References 39 publications

Trypsin‐hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects

Trypsin‐hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects

Structural and functional properties of food protein-derived antioxidant peptides

Antioxidant Peptides from the Protein Hydrolysate of Monkfish (Lophius litulon) Muscle: Purification, Identification, and Cytoprotective Function on HepG2 Cells Damage by H2O2

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