A novel antioxidative peptide derived from chicken blood corpuscle hydrolysate

Zheng, Zhaojun; Si, Daoyuan; Ahmad, Baseer; Li, Zhongxuan; Zhang, Rijun

doi:10.1016/j.foodres.2017.12.078

Cited by 51 publications

(24 citation statements)

References 58 publications

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“…Given the growing interest in using underutilized foods as inexpensive sources for the production of bioactive peptides, there has been an upsurge in the number of studies examining the antioxidant properties of peptides generated from hitherto conventionally inedible or non‐conventional foods in recent years. These include hydrolyzates and peptides from the red alga Palmaria palmata (Harnedy et al, ), processed fish wash water (Zhou et al, ), chicken blood cells (Zheng, Si, Ahmad, Li, & Zhang, ), squid pen chitosan (Shavandi et al, ), abalone viscera (Je, Park, Hwang, & Ahn, ), pearl oysters (Ma, Wu, & Li, ), rice bran (Phongthai et al, ), mulberry leaf (Sun et al, ), and silkworm (Liu, Wan, Liu, Zou, & Liao, ). Others include microorganisms and single cell organisms (Alzahrani, Perera, & Hemar, ), blood clam (Chi, Hu, Wang, Li, & Ding, ), and echinoderm byproducts (Mamelona, Saint‐Louis, & Pelletier, ).…”

Section: Production Of Antioxidant Enzymatic Protein Hydrolyzatesmentioning

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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Section: Production Of Antioxidant Enzymatic Protein Hydrolyzatesmentioning

confidence: 99%

Structural and functional properties of food protein-derived antioxidant peptides

2019

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“…The abundance of hydrophobic amino acids, such as Pro, Met, Leu, Tyr, Phe and Val in the peptide sequences seems to enhance the antioxidant activities by increasing peptide solubility in lipids, and the interaction with radical species [52][53][54]. Zheng et al reported that hydrophobic amino acid residues (Leu and Ile) in AEDKKLIQ played an important role on the hydrophobic targets [55]. Met residue acted as a reactive site in the PMRGGGGYHY, WMFDW, WMGPY, and EMGPA through formatting a sulfoxide structure to scavenge free radicals [18,56].…”

Section: Structure-activity Relationship Of Mmp-4 Mmp-7 and Mmp-12mentioning

confidence: 99%

“…Pro residue can help antioxidant peptides, such as LDEPDPL, WMGPY and EMGPA, scavenge ROS because of the pyrrolidine ring [18,57]. Furthermore, aromatic groups of Trp, Phe, and Tyr residues can scavenge free radicals by providing protons [55][56][57][58]. Therefore, hydrophobic/aromatic amino acid residues in the sequences of EDIVCW (Ile, Val, Cys and Trp), MEPVW (Met, Pro, Val and Trp), and YWDAW (Tyr, Trp, Ala and Trp) play an important role for their antioxidant activity.…”

Section: Structure-activity Relationship Of Mmp-4 Mmp-7 and Mmp-12mentioning

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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“…The antioxidant activity of the protein is closely related to its amino acid composition. Peptides containing hydrophobic amino acids can increase their solubility at the water-lipid interface and better interact with free radicals (Zheng, Si, Baseer, Li, & Zhang, 2018).…”

Section: Amino Acid Composition and Content In M Oleifera Seedsmentioning

confidence: 99%

Nutritional compositions of Indian Moringa oleifera seed and antioxidant activity of its polypeptides

Liang

Wang

et al. 2019

Food Science & Nutrition

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To study the nutritional composition of Indian Moringa oleifera seed and the antioxidant activity of M. oleifera seed polypeptide, Indian M. oleifera seed was used as raw material for composition analysis and content determination. After extraction of the seed protein, enzymatic hydrolysis with flavourzyme, dispase, papain, pepsin, and alcalase was conducted for different time, and the optimal enzymatic hydrolysis conditions was determined with DPPH scavenging capacity as an indicator. The seed polypeptides obtained by enzymatic hydrolysis were ultrafiltered, and the active peptide fragments were tracked with DPPH, HO (•OH), ABTS and superoxide anion (O 2 • − ) free radical scavenging ability and lipid oxidation inhibition rate as indicators. The results showed that the protein content in Indian M. oleifera seed was high to 40.34%, containing seven essential amino acids. The content of macroelements such as potassium, sodium, and magnesium is high, with the potassium content as high as 2,357.71 mg/kg, among the microelements, the iron content as high as 36.2 mg/kg. The optimum enzymatic hydrolysis conditions were as follows: enzymatic hydrolysis with flavourzyme (50°C, pH 6.7) for 300 min, and DPPH scavenging capacity was 84.76%. Activity tracing found that the polypeptide fragment with molecular weight <3.5 kDa had the strongest antioxidant capacity, and the EC 50 values of DPPH, •OH, ABTS, and O 2 • − free radical scavenging rates were 4.0, 4.2, 5.3, and 4.3 mg/ml, respectively. The above results show that Indian M. oleifera seed not only has high nutritional value, but its protease enzymatic hydrolyzate also has significant antioxidant activity, which can be further developed into nutrition products, healthcare products, functional foods, beauty and skin care products, liver protection drugs, etc.

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A novel antioxidative peptide derived from chicken blood corpuscle hydrolysate

Cited by 51 publications

References 58 publications

Structural and functional properties of food protein-derived antioxidant peptides

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

Nutritional compositions of Indian Moringa oleifera seed and antioxidant activity of its polypeptides

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