Comparative Study on the Antioxidant Activity of Peptides from Pearl Oyster(Pinctada martensii) Mantle Type V Collagen and Tilapia(Oreochromis niloticus) Scale Type Ⅰ Collagen

In this study, Pearl oyster mantle type V collagen(POMC) and tilapia scale type I collagen(TSC) were extracted and hydrolyzed by various proteases in order to obtain peptides. The antioxidant activity of the peptides was investigated by DPPH, hydroxyl radical scavenging experiments and a dynamic digestion model in vitro. The results show that there are significant differences in amino acid composition between POMC and TSC. The collagen peptides obtained from pearl oyster mantle(POMCP) by treating with alkaline protease exhibited higher antioxidant activity than that from tilapia scale(TSCP) treated with papaya protease, and both of them showed greater DPPH and hydroxyl radical scavenging activity than other peptides. After being separated via Sephadex G-25 chromatography, the M1 fraction isolated from POMCP, and the S1 fraction from TSCP with which both had higher molecular weights showed the strongest antioxidant activity than other fractions, and the M1 fraction exhibited stronger antioxidant activity than the S1 fraction in scavenging free-radicals and protecting cells from the oxidation damage. Furthermore, after treating the dynamic digestion system model in vitro, the DPPH and hydroxyl radical scavenging activity of the M1 fraction increased slightly. These results suggest that POMCP exhibits stronger antioxidant activity than TSCP, which means that PMOP may be a good candidate to be a potential natural antioxidant in the food-processing industry.

Antioxidant peptides encrypted in flaxseed proteome:An in silico assessment

Flaxseed proteins and antioxidant peptides(AP)encrypted in their sequences were analysed in silico with a range of bioinformatics tools to study their physicochemical properties,allergenicity,and toxicity.Nine proteases(digestive,plant and microbial sources)were assessed for their ability to release known APs from 23 mature flaxseed storage proteins using the BIOPEP database.The families of proteins identified were predominantly globulins,oleosins,and small amount of conlinin.Overall,253 APs were identified from these proteins.More peptides were released by enzymatic hydrolysis from the globulins than those from oleosins and conlinin.Compared with other enzymes studied,the plant proteases(papain,ficin,and bromelain)were found to be superior to releasing APs from the flaxseed proteins.Analysis of toxicity by ToxinPred showed that none of the peptides released was toxic.Most of the APs showed structural features that are important for antioxidation,including relatively low molecular weight(dipeptides and tripeptides only);amphipathic properties(hydrophobicity range of-0.5 to+0.5);relatively low Boman index(≤2);broad range of pI(3.7-10.8),and an abundance of antioxidant amino acid residues(e.g.glutamic acid and histidine).This study demonstrate the suitability of flaxseed proteins as a source of APs.

Peptidomic analysis of whey protein hydrolysates and prediction of their antioxidant peptides

Enzymatic hydrolysis of proteins is a breakdown process of peptide bond in proteins,releasing some peptides with potential biological functions.Previous studies on enzymatic hydrolysis of whey proteins have not identified the complete peptide profiles after hydrolysis.In this study,we reconstructed a profile of peptides from whey hydrolysates with two enzymes and different processing conditions.We also developed an ensemble machine learning predictor to classify peptides obtained from whey hydrolysis.A total of 2572 peptides were identified over three process conditions with two enzymes in duplicate.499 peptides were classified and chosen as potential antioxidant peptides from whey proteins.The peptides classified as antioxidants in the hydrolysates had a proportion of 13.1%-24.5%regarding all peptides identified.These results facilitate the selection of promising peptides involved in the antioxidant properties during the enzymatic hydrolysis of whey proteins,aiding the discovery of novel antioxidant peptides.

Tartary buckwheat(Fagopyrum tataricum(L.)Gaertn)protein-derived antioxidant peptides:mechanisms of action and structure-activity relationship in Caco-2 cell models

Excessive reactive oxygen species(ROS)can cause oxidative damage and lead to various metabolic disease.Tartary buckwheat(Fagopyrum tataricum(L.)Gaertn)is a new kind of protein-rich functional food,the protein in which has been proved to have good antioxidant capacity.In this study,in order to further explore the antioxidant mechanism of Tartary buckwheat protein,4 peptides(CR-8,LR-8,GK-10 and SR-12)were isolated and identified from it.H2 O2 was used to induce oxidative damage to Caco-2 cells to evaluate antioxidant capacity of these peptides.The results of superoxide dismutase(SOD),total antioxidant capacity(T-AOC)and mitochondrial membrane potential etc.showed that these peptides have superior antioxidant capacity.CR-8 has the best antioxidant capacity.In order to further clarify the antioxidant mechanism of CR-8,metabolomics was used to analyze related metabolites and metabolic pathways.The results showed that after CR-8 intervention,the content of metabolites such as L-acetyl carnitine has increased.This indicated that CR-8 can improve the antioxidant capacity of damaged cells by intervening in multiple metabolic pathways.This also revealed the anti-oxidant mechanism of tartary buckwheat protein.In conclusion,it provided a theoretical basis for further studying the activity of tartary buckwheat portein and utilizing buckwheat resources.

Antifatigue,Antioxidant and Immunoregulatory Effects of Peptides Hydrolyzed from Manchurian Walnut(Juglans mandshurica Maxim.) on Mice

The Manchurian walnut(Juglans mandshurica Maxim.) is rich in proteins, whereas this resource has not been used efficiently. The antifatigue, antioxidative and immunoregulatory effects of Manchurian walnut hydrolysate peptides(MWHPs)were evaluated in this study. MWHPs with a degree of hydrolysis of 32.23% were ultrafiltered and divided into three fractions,namely, high(> 10 k Da), medium(3–10 kDa), and low molecular weight(< 3 kDa), and then fed to mice continuously at doses of 200, 400 or 800 mg/(kg·d). The antifatigue, antioxidative, and immunoregulatory effects of the peptides were tested on the second and fourth weeks of MWHP administration. Results showed that low-molecular-weight MWHPs exerted significant antifatigue(prolonging swimming time, elevating liver glycogen contents, and reducing lactic acid contents), antioxidative(enhancing superoxide dismutase(SOD), GSH-Px, and catalase(CAT) activities and reducing malondialdehyde(MDA) content), and immunoregulatory(raising the immune-organ index and promoting T-lymphocyte proliferation and s Ig A secretion in the intestinal tract) effects. This research indicates that MWHPs have potential applications in health care and may be developed as a base for new functional foods.

Purification and Identification of Antioxidant Peptides from the Scallop Skirts of Mimachlamys Nobilis

The processes of scallop meats can produce a large amount of by-products like scallop skirts,which are rich in nutrients. This work aimed to obtain the information about antioxidant peptides derived from scallop skirts of Mimachlamys nobilis. The hydro-lysates obtained by trypsin exhibited the highest antioxidant activity( 75.6%,79.5% and 76.7% using DPPH,hydroxyl and superoxide anion radical scavenging activity assays,respectively). The antioxidant peptides( MNAP) were separated and purified using UF membranes,GFC processes and RP-HPLC,and the antioxidant activity of MNAP was identified to be 85.7% using DPPH radical scavenging activity assay. The peptides( MNAP) were composed of two peptides with their molecular weights2 855.6 Da and 3 007.2 Da using MALDI-TOF-MS,respectively. The results suggested that the scallop skirts of Mimachlamys nobilis could be explored as a source of antioxidant peptides.

Changes of the Content and Antioxidant Activity of Natural Peptides in Germinated Soybeans

[ Objective] This study aimed to investigate the content and antioxidant activity of natural peptides in various soybean sprouts during the germination process. [Method] By using black soybean sprouts, yellow soybean sprouts and green soybean sprouts as raw materials, the content, DPPH ·clearance rate, OH · clearance rate and reduction capacity of natural peptides in various soybean sprouts at different germination time were determined, to evaluate the antioxidant capacity of natural peptides and compare it with that of Vc. [ Result] The results showed that the contents of natural peptides in black soybean sprouts, yellow soybean sprouts and green soybean sprouts varied at different germination time. To be specific, the content of natural peptides in black soybean sprouts reached the maximmn of 0. 194 mg/g at 2 d post-germination; the content of natural pepfides in yellow soybean sprouts reached the maximum of 0.231 mg/g at 2 d post-germination; the content of natural peptides in green soybean sprouts exhibited a negative correlation with the germination time, which reached the maximum of 0. 164 mg/g at 1 d post-germination. [ Conclusion] According to the determination of DPPH ·clearance rate, OH ·clearance rate and reduction capacity of natural peptides in three varieties of soybean sprouts, natural peptides in yellow soybean sprouts possess the highest antioxidant activity, followed by those in black soybean

In vitro Antioxidant Effects of Porphyra haitanensis Peptides on H_2O_2-Induced Damage in HepG2 Cells

In this study,protein from Porphyra haitanensis was used as raw material to prepare an antioxidant peptide,and its antioxidant activity was evaluated in vitro.A model of H_2O_2-induced oxidative damage in Hep G2 cells was established,and the effects of Porphyra haitanensis hydrolysates (PHHs) on superoxide dismutase (SOD) activity and malondialdehyde (MDA) content were detected.Finally,the structure of PHHs was identified by ESI-MS/MS.The results showed that the 1,1-diphenyl-2-pyridylhydrazine(DPPH)-free radical-scavenging ability of PHHs was the strongest (59.28%at 1.0 mg m L~(-1)) when hydrolyzed with an acidic protease for 4 h.PHHs with different concentrations had protective effects on H_2O_2-induced damage to Hep G2 cells,and the protective effect was enhanced with increasing concentrations.When the level was 400μg m L~(-1),the cell survival rate was as high as 88.62%.Moreover,PHHs can significantly reduce oxidative damage to Hep G2 cells by H_2O_2,improve SOD activity,and reduce MDA content.The tetrapeptide Asp-Lys-Ser-Thr,with a molecular weight of 448 Da,was identified as an important fraction of PHHs by high-resolution mass spectrometry.

Antarctic krill antioxidant peptides show inferior IgE-binding ability and RBL-2H3 cell degranulation

Enzymatic hydrolysis,isolation,and purification might make a great deal of difference in antioxidant activity and antigenicity of peptide components.This study aimed to isolate and purify antioxidant peptide components from Antarctic krill and evaluate their allergenicity of them.Electron paramagnetic resonance(EPR)spectroscopy results indicated 3-10 kDa Antarctic krill hydrolysates(AKHs)had higher DPPH and·OH radical scavenging rates.And the second component(N2-2)purified 3-10 kDa hydrolysate showed better ability to scavenge DPPH and·OH radicals(P<0.05),which were(47.43±2.18)%and(34.33±1.25)%,respectively.Additionally,indirect-ELISA results revealed that N2-1 had a weaker ability to bind specific IgE and that N2-2 had a lower binding capability to specific IgG1(P<0.05).And N2-2 had a higher EC50 value of(5.29±0.95)ng/mL(P<0.05)in cell degranulation assay,which was about 13.80 times that of Antarctic krill.Therefore,N2-2 might be the potential source of the antioxidant peptides with lower allergenicity.

Solid-Phase Enzymatic Peptide Synthesis to Produce an Antioxidant Dipeptide

Peptide bond synthesis is favorable to the production of bioactive small peptides. However, the abuse of toxic reagents remains an issue for chemical synthesis method, whereas the low product yield and purity limit the widespread use of enzymatic method. In this study, a new solid-phase enzymatic peptide synthesis(SPEPS) strategy was developed to produce an antioxidant tyrosine-alanine dipeptide(Tyr-Ala) by using recombinant carboxypeptidase Y(CPY) as the catalyst. The general SPEPS procedure involves three steps. First, the N-protected acyl donor was covalently attached to solid resin. Second,the peptide bond was condensed between the acyl donor and the nucleophile under the catalysis of CPY. Finally, one-step cleavage was performed to remove the protecting group and cleave the peptides from solid resin. Upon the optimization of reaction conditions, 77.92%(±2.723%) yield of Tyr-Ala with high product purity of 90.971%(±2.695%) was obtained.In addition, the antioxidant activity of Tyr-Ala was determined by ABTS method, indicating that the synthesized Tyr-Ala obtained by SPEPS showed a superior antioxidant capability compared with commercial glutathione.

Production and Purification of Antioxidant Peptides from Flatfish Skin Protein Hydrolysates

Antioxidant peptides of flatfish skin protein hydrolyzed by four enzymes （Papain, Pepsin, Trypsin and Neutrase, respectively）were investigated. The Trypsin hydrotysate obtained by hydrolysis exhibited the highest 1,1- dipheny-l-2-picrylhydrazyl（DPPH） radical scavenging activity （DRSA） compared with other hydrolysates. Re- sponse surface method ology （RSM）, based on Box-Behnken design, was used to study the influence of hydrolysis conditions on the DRSA. The optimal hydrolysis conditions were as follows： pH 7.38, temperature 48.2~C and en- zyme/substrate （E/S）ratio 2 840 U/g. Under these conditions, the maximum DRSA was （22.85 ＋ 0.57）%. The experimental values agreed with the value （23.09%） predicted by the model within a 95% confidence interval. By using gel filtration chromatography and reversed-phase high performance liquid chromatography （RP-HPLC）, anti- oxidant peptide （D2-P）was isolated from flatfish skin protein hydrolysates （FSPH）and could exhibit a （54.28 ± 1.37） % scavenging activity on DPPH radical at the concentration of 5 mg/mL. This is the first report of a scientific basis for the preparation of antioxidant peptides from flatfish skin. The results suggested that the antioxidant pep- tides can be exploited into functional foods or used as a novel source of nutraceuticals.

Novel Antioxidant Peptides Derived from Enzymatic Hydrolysates of Macadamia Protein

In the present work, macadamia protein was enzymatic hydrolyzed to produce peptides which had abundant antioxidant activities. The relative antioxidant capacity was investigated through some in vitro models such as scavenging activity of DPPH radical, scavenging of ABTS+ radical and evaluation of the total antioxidant capacity assay. Macadamia protein was characterized by methods of DEAE cellulose cation-exchange chromatography and SDS-PAGE. Besides, method of price graph was used to compare the difference and to investigate the connection between the actual and ideal antioxidant value of the hydrolysates, aiming to reduce this difference.

Kinetically Controlled Carboxypeptidase-Catalyzed Synthesis of Novel Antioxidant Dipeptide Precursor BOC-Tyr-Ala

Recently, enzymatic peptide synthesis has drawn increasing attention due to its eco-friendly reagents and mild conditions, as compared to traditional chemical peptide synthesis. In this study, we successfully produced an important antioxidant dipeptide precursor, BOC-Tyr-Ala, via a kinetically controlled enzymatic peptide synthesis reaction, catalyzed by the recombinant car- boxypeptidase Y （CPY） expressed in P. pastoris GS 115. In this reaction, the enzyme activity was 95.043 U/mL, and we used t-butyloxycarbonyl-L-tyrosine-methyl ester （BOC-Tyr-OMe） as the acyl donor and L-alanine （L-Ala） was the amino donor. We optimized the reaction conditions to be： 30 ℃, pH 9.5, organic phase （methanol）/aqueous phase = 1：20, BOC-Tyr-OMe 0.05 mol/L, Ala 0.5 mol/L, and a reaction time of 12 h. Under these conditions, the dipeptide yield reached 49.84%. Then, we established the kinetic model of the synthesis reaction in the form of Michaelis-Menten equation according to the con-centration-time curve during the process and the transpeptidation mechanism. We calculated the apparent Michaelis constant K^（app）mand the apparent maximum reaction rate r^（app）max to be 2.9946 x 10^-2 mol/L and 2.0406 x 10.2 mmol/（mL h）, respectively.

Study on the Molecular Weight Composition and Antioxidant Activity of Peanut Bioactive Peptides

[ Objective] To prepare peanut bioactive peptides and analyze their molecular weight composition and antioxidant activity. [ Method ] The dialysis bag of 8.0, 3.5 and 1.0 kD were used to classify the hydrolyzate derived from alcalase and flavourzyme, peanut bioactive poptides of differ-ent molecular weight were obtained and then their scavenging capacity of free radicals was measured. The molecular weight composition was stud-ied by Tricine-SDS-PAGE.[Result] The content of peptides 〈 1.0 kD were 76.21% and 83.42% in the total hydrolyzate from alcalase and fla-vourzyme respectively. All hydrolyzate with different molecular grades showed free radical scavenging capacity, which was increased with the reduc- tion of molecular mass. The peptides 〈 1.0 kD exhibited higher radical scavenging capacity of （87.41 ±0.66） % （alcalase） and （67.88 ±0.48）% （ flavourzyme）, respectively. [ Conclusion] Peanut bioactive peptides had strong effect of antioxidant capacity, especially that 〈 1.0 kD, which had great prospect.

Effects of Small Peptide Chelated Copper,Iron,Manganese and Zinc on Growth Performance,Chicken Quality and Antioxidant Capacity of Yellow Feather Broilers

[Objective]The paper was to study effects of small peptide chelated trace elements(copper,iron,zinc and manganese)on growth performance,chicken quality and antioxidant capacity of rapid yellow feather broilers.[Method]Three hundred one-day-old yellow feather broilers with similar body weight were selected and randomly divided into three treatments:inorganic trace element group(basal diet+inorganic trace elements),organic trace element group(basal diet+small peptide chelated trace elements)and compound group(basal diet+50%inorganic trace elements+50%small peptide chelated trace elements).There were 10 replicates per treatment and 10 chickens per replicate.The trial lasted for 63 d.[Result]①Compared to inorganic trace element group,average daily gain(ADG)of yellow feather broilers in organic trace element group was significantly increased over the whole period(P<0.05).②There was no significant difference in slaughter performance and immune organ indices among the three test groups(P>0.05).③There was no significant difference in breast muscle pH,chicken color,drip loss,and shear force among the three groups(P>0.05),but cooking loss of chicken breast in inorganic trace element group was 27.46%and 22.53%higher than those in organic trace element group and compound group,respectively(P<0.05).④MDA content in serum in organic trace element group was 15.61%lower than that in inorganic trace element group(P<0.05).[Conclusion]Complete substitution of inorganic copper,iron,zinc and manganese by small peptide chelated copper,iron,zinc,and manganese significantly increases ADG of broilers,improves quality of chicken breast,and enhances antioxidant capacity.

Antioxidant Activity of Peptides Obtained from Cotton Ground Oil-Cake Proteins

Antioxidant activity of the peptides derived from proteins of defatted cottonseed kernels and cotton ground oil-cake by their enzymatic hydrolysis with acidic （Asp. niger） and neutral proteinases （Bac. amyloliquefaciens） was studied. Antioxidant activity of the derived peptides depended on the used proteins and enzymes. The peptides derived by using of neutral proteinase possessed higher antioxidant activity, in comparison with the peptides derived by acidic proteinases.

Preparation and Antioxidative Effects of Soybean Peptides

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Effects of Peptides from Swine Blood on Antioxidative Capacity of Mice

Porcine peptides have strong antioxidative activities. The porcine peptides at different doses were administered hepatotoxic mice to investigate their in vivo antioxidant capability. After administration, the activity of superoxide dismutase and glutathione peroxidase in liver and serum was enhanced and malonaldehyde content in liver and serum was greatly decreased. Therefore, the porcine peptides can significantly reduce the damage of active oxygen to body, enhance the body＇s antioxidant capability, and thus maintain health.

Identifcation and characterization of novel dual-function antioxidant and umami peptides from protein hydrolysates of Huangjiu lees

Objectives:Lees are the major by-product of Huangjiu brewing and are prone to decomposition due to abundant protein residues.This study aims to convert the lees into high-value peptides with umami and antioxidant difunctionals.Materials and Methods:Herein,a one-step hydrolysis method combined with favorzyme followed by amylase pretreatment was developed and optimized.The target peptide fraction was collected and evaluated after ultrafltration and ethanol precipitation,and then identifed by nanohigh-performance liquid chromatography-tandem mass spectrometry.The target peptides were fltered through virtual screening,sensory,and radical scavenging verifcation.Results:The results show that 80 U/g amylase and 3500 U/g favorzyme synergistic hydrolysis at 50°C for 3 h performed best for umami intensity and antioxidant activity.A total of 5266 peptides was identifed from the 80%ethanol precipitation fraction,fnally secreened 7 umami peptides.The umami recognition threshold of the 7 peptides ranged from 0.38 to 0.66 mmol/L in water.Among them,DPDGW and DNPNW exhibited good DPPH antioxidant ability with IC_(50) values of 0.6982 mg/mL and 0.4315 mg/mL,respectively.Additionally,molecular docking studies indicated that all umami peptides tend to interact with the T1R3 receptor through hydrogen bonds and van der Waals forces,involving key residues such as ASN68,SER104,HIS145,SER276,VAL277,GLU301,ALA302,THR305,and HIS387.Conclusion:This study shows that Huangjiu lees is a potential resource for favor and bioactive peptide development,which provides a reference for other waste protein recycling.

Antioxidant soy peptide can inhibit xanthine oxidase activity and improve LO_(2) cell damage

In this study,SHECN(Ser-His-Glu-Cys-Asn)and SHCMN(Ser-His-Cys-Met-Asn)soybean peptides were used as the research objects to investigate their antioxidant activities and XO(xanthine oxidase)activity reduction effects.The results show that SHECN and SHCMN have strong antioxidant activities,and at the same time protect the oxidative stress damage caused by HUA(hyperuricemia).They can quench XO,change the secondary structure of XO,and reduce its activity,which leads to the reduction of UA(uric acid)levels.Molecular docking demonstrated soybean peptides could bind to XO target proteins,respectively.In this study,SHECN and SHCMN were obtained from soybean peptides.Based on the data,soy peptides may be an attractive natural ingredient for the development of novel functional foods that inhibit XO activity.