Antioxidant Activity of Oat Proteins Derived Peptides in Stressed Hepatic HepG2 Cells

Du, Yichen; Esfandi, Ramak; Willmore, William G.; Tsopmo, Apollinaire

doi:10.3390/antiox5040039

Cited by 63 publications

(63 citation statements)

References 37 publications

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“…The IC50 for DPPH free radical scavenging of TSPH (produced in optimized conditions) 0.831 mg/ml was significantly lower compared to that of non‐digested proteins (UTSP, 2.677 mg/ml). Enzymatic hydrolysis of food proteins with alcalase have been demonstrated in other studies to enhance antioxidant activities due several factors including the size of peptides, the presence of tyrosine, tryptophan, histidine, or the overall hydrophobicity (Du, Esfandi, Willmore, & Tsopmo, ; Jodayree et al, ).

Y = - 9.554 + 0.714 X_{1} - 4.6293 X_{2} - 0.0031 X_{1}^{2} + 4.6448 X_{2}^{2} + 0.01 X_{1} X_{2}

…”

Section: Resultsmentioning

confidence: 99%

Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins

et al. 2018

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The objective of this was to determine the impact of enzymatic hydrolysis on the multifunctionality of tomato seed protein hydrolysates (TSPH) and their physicochemical properties. The enzymatic hydrolysis was performed using alcalase and two factors response surface methodology. The best conditions were 131.4 min and 3% enzyme/substrate (E/S) for antioxidant activity; 174.5 min and 2.93% E/S for angiotensin‐converting enzyme (ACE) inhibition; and 66.79 min and 2.27% E/S for the calcium binding. Antioxidant and ACE hydrolysates were characterized by higher solubility, zeta potential, and thermal stability while properties of the calcium binding hydrolysate were only minimally affected by the enzymatic hydrolysis. Gel electrophoresis showed that molecular weights of polypeptides in the calcium binding TSPH were higher compared to those in ACE and antioxidant TSPHs. This was due to the low degree of hydrolysis of the calcium binding hydrolysate. Practical applications Nowadays, different protein sources are used to produce protein hydrolysates containing bioactive peptides that can help alleviate oxidation of foods, oxidative stress, and chronic conditions (e.g., hypertension, diabetes, cardiovascular disorder). Hydrolyzed proteins also have the potential to increase mineral absorption through the formation of mineral‐binding complexes. Biological activities of proteins and peptides from tomato processing byproduct (i.e., pomace) have received until now little attention. The determination of physicochemical properties and biological activities of the hydrolyzed proteins has application in the formulation of value‐added food products for the reduction of oxidative stress and risks of developing chronic diseases. In addition, there will be a reduction of pomace waste generated by the tomato processing industry.

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Y = - 9.554 + 0.714 X_{1} - 4.6293 X_{2} - 0.0031 X_{1}^{2} + 4.6448 X_{2}^{2} + 0.01 X_{1} X_{2}

…”

Section: Resultsmentioning

confidence: 99%

Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins

et al. 2018

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“…In this assay, dialysis of Visc/Flav sample did not affect cell viability. In a previous study, similar results were observed using purified oat peptides; however, the results were more uniformly distributed throughout the samples, possibly due to the purity of the samples [247]. The variation among OBPI and OBPH treated samples might be due to the existence of peptides fragments in hydrolysates and possibly the presence of small molecules like secondary metabolites, polysaccharides, and salts [248], [249], [250].…”

Section: Iron Chelating Activitysupporting

confidence: 77%

“…Treatment with OBPH also enhanced GPX activity, but not significantly higher than that of NEG control. In the previous study, some purified oat bran hydrolysates were able to increase GPx activity in HepG2 cells greater than that of NEG control [247]. The low activity of GPx in this study might be due to susceptibility to damage of GPx enzyme to hydrogen peroxide itself in presence of sample impurities [266].…”

Section: Antioxidant Enzymesmentioning

confidence: 48%

“…Treating biological systems with protein hydrolysates showed improvement in the activity level of SOD, reducing the adverse effects of oxidative stress [270], [271]. All OBPHs could restore SOD activity in HepG2 cells more significantly compared to the previous study [247]. It is possible that production of a broad range of antioxidative peptides resulted in increased expression of SOD.…”

Section: Antioxidant Enzymesmentioning

confidence: 78%

“…For this part, OBPHs were selected based on their performance from chemistry based and MTT assays. HepG2 cells with oat protein hydrolysates can affect the activity of antioxidant enzymes [247].…”

Section: Antioxidant Enzymesmentioning

confidence: 99%

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Antioxidant and Antiapoptotic Properties of Oat Bran Protein Hydrolysates in AAPH-Induced Oxidative Stress Hepatocarcinoma HepG2

Esfandi¹

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The onset of many chronic diseases such as cancer, carcinogenesis, cardiovascular disease, and several other health problems, involves oxidative stress damage to biomolecules such as DNA, lipid, and proteins. There have been many preventative and therapeutic methods proposed to increase cellular defense mechanisms against oxidative damage such as using bioactive peptide with antioxidant activities from food sources. This study found that AAPH-induced oxidative stress in human hepatocarcinoma HepG2 cells caused changes in cellular morphological features and functionalities such as cell viability, activity of antioxidative enzymes (catalase (CAT), glutathione peroxidase (GPx), and superoxide dismutase (SOD)), production of reactive oxygen species (ROS), and rate of apoptosis. The use of oat bran protein hydrolysates restored some of the properties to normal values (i.e., control cells). In this work, oat brans were treated with two carbohydrases (Cellulase ® (Cell) and viscozyme ® L (Visc) which cleave cell wall polysaccharides and produce oat bran protein isolates (OBPIs) with protein contents. OBPI was subsequently treated with proteases Alcalase (Alca), Flavourzyme ® (Flav), Papain (Papa) and Protamex (Prot) to produce four oat bran protein hydrolysates (OBPHs) from each of oat bran protein isolate (OBPIs). Antioxidative effects of both the two OBPI and four OBPH samples were studied in chemistry and HepG2 cell cultures assays. In the chemistry assays the antioxidative activities were determined using oxygen radical absorbance capacity (ORAC), 2,2'-azino-bis (3ethylbenzothiazoline-6-sulphonic acid) or ABTS •+ , radical, hydroxyl ( • OH), and superoxide anion (O2 •-) radical scavenging assays. Data from oxygen radical absorbance capacity (ORAC) and 2,2'azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS •+ ) assays were expressed as Trolox (a water-soluble vitamin E analogue) equivalent per gram (TE/g) of the sample followed the same pattern. The highest ORAC activities were observed in Cell/Papa (417.0 ± 5.1 TE/g), Visc/Flav (406.0 ± 8.8 TE/g) and Visc/Papa (397.0 ± 13.9 TE/g) while in the ABTS •+ , highest scavenging samples were Visc/Flav and Visc/Papa (863.80 ± 20.3 and 814.8 ± 17.2 TE/g respectively). In the hydroxyl radical scavenging assay, Cellulase and Viscozyme OBPIs significantly prevented the formation of • OH, radicals 38.5 ± 0.8 and 36.0 ± 0.4%, respectively compared to all hydrolysates. iii Superoxide anion radical scavenging activity was the highest in samples Visc/Alca and Cell/Prot both at 37.3 ± 0.9%. SDS-PAGE results indicated that globulin (58 kDa) was the main protein in OPBIs and those hydrolysates did not contain protein or fragments above 15 kDa. Cytotoxicity of OBPIs and OBPHs, their ability to reduce intracellular reactive oxygen species (ROS), and regulate the activity of three main antioxidant enzymes were evaluated in the AAPH-induced oxidative stress of HepG2 cells. Cytotoxic effect OBPH was evaluated using Visc/Flav ND at 50 -400 µg/mL. No cytotoxicity was observed in MTT (3-...

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Cereal Proteins: Potential Health Applications and Allergenicities

Bleakley

2018

Novel Proteins for Food, Pharmaceuticals and Agriculture

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Antioxidant Activity of Oat Proteins Derived Peptides in Stressed Hepatic HepG2 Cells

Cited by 63 publications

References 37 publications

Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins

Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins

Antioxidant and Antiapoptotic Properties of Oat Bran Protein Hydrolysates in AAPH-Induced Oxidative Stress Hepatocarcinoma HepG2

Cereal Proteins: Potential Health Applications and Allergenicities

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