scholarly journals Four Antioxidant Peptides from Protein Hydrolysate of Red Stingray (Dasyatis akajei) Cartilages: Isolation, Identification, and In Vitro Activity Evaluation

Marine Drugs ◽  
2019 ◽  
Vol 17 (5) ◽  
pp. 263 ◽  
Author(s):  
Xiao-Yang Pan ◽  
Yu-Mei Wang ◽  
Li Li ◽  
Chang-Feng Chi ◽  
Bin Wang
Keyword(s):  
Protein Hydrolysate ◽  
Guanidine Hydrochloride ◽  
Cation Radical ◽  
Reducing Power ◽  
Amino Acid Sequences ◽  
Water Soluble ◽  
Antioxidant Peptides ◽  
Antioxidant Additive ◽  
Dasyatis Akajei ◽  
Red Stingray

In the work, water-soluble proteins of red stingray (Dasyatis akajei) cartilages were extracted by guanidine hydrochloride and hydrolyzed using trypsin. Subsequently, four antioxidant peptides (RSHP-A, RSHP-B, RSHP-C, and RSHP-D) were isolated from the water-soluble protein hydrolysate while using ultrafiltration and chromatographic techniques, and the amino acid sequences of RSHP-A, RSHP-B, RSHP-C, and RSHP-D were identified as Val-Pro-Arg (VPR), Ile-Glu-Pro-His (IEPH), Leu-Glu-Glu--Glu-Glu (LEEEE), and Ile-Glu-Glu-Glu-Gln (IEEEQ), with molecular weights of 370.46 Da, 494.55 Da, 647.64 Da, and 646.66 Da, respectively. VPR, IEPH, LEEEE, and IEEEQ exhibited good scavenging activities on the DPPH radical (EC50 values of 4.61, 1.90, 3.69, and 4.01 mg/mL, respectively), hydroxyl radical (EC50 values of 0.77, 0.46, 0.70, and 1.30 mg/mL, respectively), superoxide anion radical (EC50 values of 0.08, 0.17, 0.15, and 0.16 mg/mL, respectively), and ABTS cation radical (EC50 values of 0.15, 0.11, 0.19, and 0.18 mg/mL, respectively). Among the four isolated antioxidant peptides, IEPH showed the strongest reducing power and lipid peroxidation inhibition activity, but LEEEE showed the highest Fe2+-chelating ability. The present results suggested that VPR, IEPH, LEEEE, and IEEEQ might have the possibility of being an antioxidant additive that is used in functional food and pharmaceuticals.

scholarly journals Preparation, Identification, and Activity Evaluation of Eight Antioxidant Peptides from Protein Hydrolysate of Hairtail (Trichiurus japonicas) Muscle

Marine Drugs ◽  
2019 ◽  
Vol 17 (1) ◽  
pp. 23 ◽  
Author(s):  
Xiu-Rong Yang ◽  
Lun Zhang ◽  
Dong-Ge Ding ◽  
Chang-Feng Chi ◽  
Bin Wang ◽  
...  
Keyword(s):  
Superoxide Anion ◽  
Protein Hydrolysate ◽  
Reducing Power ◽  
Model System ◽  
Amino Acid Sequences ◽  
Health Food ◽  
Antioxidant Peptides ◽  
Food Industries ◽  
Molecular Weights ◽  
Hydrolysis Process

In this report, protein of hairtail (Trichiurus japonicas) muscle was separately hydrolyzed using five kinds of proteases (alcalase, trypsin, neutrase, pepsin, and papain), and the papain- and alcalase-hydrolysates showed higher 2,2-diphenyl-1-picrylhydrazyl radicals (DPPH•) and hydroxyl radical (HO•) scavenging activity than other three protease hydrolysates. Therefore, the protein hydrolysate of hairtail muscle (HTP) was prepared using binary-enzymes hydrolysis process (papain + alcalase). Subsequently, eight antioxidant peptides were purified from HTP using membrane ultrafiltration and chromatography technology, and their amino acid sequences were identified as Gln-Asn-Asp-Glu-Arg (TJP1), Lys-Ser (TJP2), Lys-Ala (TJP3), Ala-Lys-Gly (TJP4), Thr-Lys-Ala (TJP5), Val-Lys (TJP6), Met-Lys (TJP7), and Ile-Tyr-Gly (TJP8) with molecular weights of 660.3, 233.0, 217.1, 274.1, 318.0, 245.1, 277.0, and 351.0 Da, respectively. TJP3, TJP4, and TJP8 exhibited strong scavenging activities on DPPH• (EC50 0.902, 0.626, and 0.663 mg/mL, respectively), HO• (EC50 1.740, 2.378, and 2.498 mg/mL, respectively), superoxide anion radical (EC50 2.082, 2.538, and 1.355 mg/mL, respectively), and 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical (EC50 1.652, 0.831, and 0.586 mg/mL, respectively). Moreover, TJP3, TJP4, and TJP8 showed higher reducing power and inhibiting ability on lipid peroxidation in a linoleic acid model system. These results suggested that eight isolated peptides (TJP1 to TJP8), especially TJP3, TJP4, and TJP8 might serve as potential antioxidants applied in the pharmaceutical and health food industries.

scholarly journals Purification and Characterization of Antioxidant Peptides Derived from Protein Hydrolysate of the Marine Bivalve Mollusk Tergillarca granosa

Marine Drugs ◽  
2019 ◽  
Vol 17 (5) ◽  
pp. 251 ◽  
Author(s):  
Xiu-Rong Yang ◽  
Yi-Ting Qiu ◽  
Yu-Qin Zhao ◽  
Chang-Feng Chi ◽  
Bin Wang
Keyword(s):  
Protein Hydrolysate ◽  
Cation Radical ◽  
Amino Acid Sequences ◽  
Marine Bivalve ◽  
Antioxidant Peptides ◽  
Food Ingredient ◽  
Molecular Weights ◽  
Ph Conditions ◽  
Blood Cockle

In this report, protein hydrolysate (TGH) of blood cockle (Tegillarca granosa) was prepared using a two-enzyme system (Alcalase treatment for 1.5 h following Neutrase treatment for 1.5 h). Subsequently, six antioxidant peptides were isolated from TGH using ultrafiltration and chromatography methods, and their amino acid sequences were identified as EPLSD, WLDPDG, MDLFTE, WPPD, EPVV, and CYIE with molecular weights of 559.55, 701.69, 754.81, 513.50, 442.48, and 526.57 Da, respectively. In which, MDLFTE and WPPD exhibited strong scavenging activities on DPPH radical (EC50 values of 0.53 ± 0.02 and 0.36 ± 0.02 mg/mL, respectively), hydroxy radical (EC50 values of 0.47 ± 0.03 and 0.38 ± 0.04 mg/mL, respectively), superoxide anion radical (EC50 values of 0.75 ± 0.04 and 0.46 ± 0.05 mg/mL, respectively), and ABTS cation radical (EC50 values of 0.96 ± 0.08 and 0.54 ± 0.03 mg/mL, respectively). Moreover, MDLFTE and WPPD showed high inhibiting ability on lipid peroxidation. However, MDLFTE and WPPD were unstable and could not retain strong antioxidant activity at high temperatures (>80 °C for 0.5 h), basic pH conditions (pH > 9 for 2.5 h), or during simulated GI digestion. In addition, the effect of simulated gastrointestinal digestion on TGP4 was significantly weaker than that on MDLFTE. Therefore, MDLFTE and WPPD may be more suitable for serving as nutraceutical candidates in isolated forms than as food ingredient candidates in functional foods and products.

scholarly journals Identification and Characterization of Novel Antioxidant Protein Hydrolysates from Kiwicha (Amaranthus caudatus L.)

Antioxidants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 645
Author(s):  
Sergio Montserrat-de la Paz ◽  
Alicia Martinez-Lopez ◽  
Alvaro Villanueva-Lazo ◽  
Justo Pedroche ◽  
Francisco Millan ◽  
...  
Keyword(s):  
Antioxidant Capacity ◽  
Reducing Power ◽  
Protein Isolate ◽  
Protein Hydrolysates ◽  
Antioxidant Peptides ◽  
Amaranthus Caudatus ◽  
Intact Proteins ◽  
Identification And Characterization

Kiwicha (Amaranthus caudatus) is considered one of the few multipurpose pseudocereals for its potential use not only as a source of nutrients and fiber but also for its bioactive compounds. In recent years, antioxidant peptides are commonly used as functional ingredient of food. Herein, a kiwicha protein isolate (KPI), obtained from kiwicha defatted flour (KDF), was hydrolyzed by Bioprotease LA 660, a food-grade endoprotease, under specific conditions. The resulting kiwicha protein hydrolysates (KPHs) were chemically characterized and their digestibility and antioxidant capacity were evaluated by in vitro cell-free experiments owing to their measure of capacity to sequester DPPH free radical and reducing power. KPHs showed higher digestibility and antioxidant capacity than intact proteins into KPI. Therefore, the results shown in this study indicate that KPHs could serve as an adequate source of antioxidant peptides, representing an effective alternative to the generation of functional food.

Antioxidant Activity of Peptides Extracted from Brewers’ Spent Grain Peptides

2012 ◽  
Vol 554-556 ◽  
pp. 891-899
Author(s):  
Xu Yan Zong ◽  
Li Li ◽  
Xu Qiao Feng ◽  
Hui Bo Luo ◽  
Jian Zhou ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Nutritive Value ◽  
Superoxide Radical ◽  
Reduced Glutathione ◽  
Protein Hydrolysate ◽  
Low Cost ◽  
Reducing Power ◽  
Gel Permeation Chromatography ◽  
Cosmetic Products ◽  
Spent Grain

Brewer’s spent grain (BSG) protein extracted from BSG was hydrolyzed using Alcalase to produce BSG protein hydrolysate. BSG protein hydrolysate was fractionated by ultrafiltration to obtain brown color BSG peptides. Antioxidant activity of BSG peptides was analyzeded and compared with reduced glutathione (GSH). BSG peptides exhibited 50% of scavenging activities on 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, hydroxyl radical, and superoxide radical with concentrations less than 0.8 mg/mL, 0.6 mg/mL and 0.6 mg/mL, respectively. The reducing power of BSG peptides was 0.70 at the concentration of 2.00 mg/mL. 86.30% of the total amount of the BSG peptides purified by gel permeation chromatography was below 2000 Da. Because of its antioxidant activity, stability, nutritive value and low cost, BSG peptides exerts a possibility to use in food or cosmetic products.

Isolation and Structural Characterization of Antioxidant Peptides from Degreased Apricot Seed Kernels

2018 ◽  
Vol 101 (5) ◽  
pp. 1661-1663 ◽  
Author(s):  
Haisheng Zhang ◽  
Jing Xue ◽  
Huanxia Zhao ◽  
Xinshuai Zhao ◽  
Huanhuan Xue ◽  
...  
Keyword(s):  
Amino Acid ◽  
Antioxidant Activities ◽  
Gel Filtration ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Seed Kernel ◽  
Antioxidant Peptides ◽  
Food Preservatives ◽  
Isolation And Purification ◽  
Rp Hplc

Abstract Background: The composition and sequence of amino acids have a prominent influence on the antioxidant activities of peptides. Objective: A series of isolation and purification experiments was conducted to explore the amino acid sequence of antioxidant peptides, which led to its antioxidation causes. Methods: The degreased apricot seed kernels were hydrolyzed by compound proteases of alkaline protease and flavor protease (3:2, u/u) to prepare apricot seed kernel hydrolysates (ASKH). ASKH were separated into ASKH-A and ASKH-B by dialysis bag. ASKH-B (MW < 3.5 kDa) was further separated into fractions by Sephadex G-25 and G-15 gel-filtration chromatography. Reversed-phase HPLC (RP-HPLC) was performed to separate fraction B4b into two antioxidant peptides (peptide B4b-4 and B4b-6). Results: The amino acid sequences were Val-Leu-Tyr-Ile-Trp and Ser-Val-Pro-Tyr-Glu, respectively. Conclusions: The results suggested that ASKH antioxidant peptides may have potential utility as healthy ingredients and as food preservatives due to their antioxidant activity. Highlights: Materials with regional characteristics were selected to explore, and hydrolysates were identified by RP-HPLC and matrix-assisted laser desorption ionization-time-of-flight-MS to obtain amino acid sequences.

scholarly journals Antioxidant, Antiproliferative and Apoptosis-Inducing Efficacy of Fractions from Cassia fistula L. Leaves

Antioxidants ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 173 ◽  
Author(s):  
Sandeep Kaur ◽  
Ajay Kumar ◽  
Sharad Thakur ◽  
Kapil Kumar ◽  
Ritika Sharma ◽  
...  
Keyword(s):  
Glycogen Synthase ◽  
Apoptotic Cell ◽  
Radical Scavenging ◽  
Cation Radical ◽  
Reducing Power ◽  
B Cell Lymphoma ◽  
Expression Level ◽  
Cassia Fistula ◽  
Nitric Oxide Radical ◽  
Mitochondrial Membrane Depolarization

Cassia fistula L. is a highly admirable traditional medicinal plant used for the treatment of various diseases and disorders. The present study was performed to divulge the antioxidant, antiproliferative, and apoptosis-inducing efficacy of fractions from C. fistula leaves. The hexane (CaLH fraction), chloroform (CaLC fraction), ethyl acetate (CaLE fraction), n-butanol (CaLB fraction), and aqueous (CaLA fraction) were sequentially fractionated from 80% methanolic (CaLM extract) of C. fistula leaves. The CaLE fraction was fractionated using column chromatography to yield a pure compound, which was characterized as Epiafzelechin (CFL1) based on 1H, 13C, and DEPT135 NMR. Among these fractions, CaLE and isolated CFL1 fractions exhibited an effective antioxidant potential in Ferric ion reducing power, (2,2’-azino-bis (3-ethylbenzothiazoline -6-sulfonic acid)) cation radical scavenging, and nitric oxide radical scavenging assays. Epiafzelechin was investigated for its antiproliferative effects against MG-63 (osteosarcoma), IMR-32 (neuroblastoma), and PC-3 (prostate adenocarcinoma), and was found to inhibit cell proliferation with a GI50 value of 8.73, 9.15, and 11.8 μM respectively. MG-63 cells underwent apoptotic cell death on treatment with Epiafzelechin as the cells showed the formation of apoptotic bodies, enhanced reactive oxygen species (ROS) generation, mitochondrial membrane depolarization along with an increase in early apoptotic cell population analyzed using Annexin V-FITC/PI double staining assay. Cells showed cell cycle arrest at the G0/G1 phase accompanied by a downregulation in the expression levels of p-Akt (Protein kinase B), p-GSK-3β (Glycogen synthase kinase-3 beta), and Bcl-xl (B-cell lymphoma-extra large) proteins. RT-PCR (Real time-polymerase chain reaction) analysis revealed downregulation in the gene expression level of β-catenin and CDK2 (cyclin-dependent kinases-2) while it upregulated the expression level of caspase-8 and p53 genes in MG-63 cells.

scholarly journals Formulation of Ethyl Cellulose Microparticles Incorporated Pheophytin A Isolated from Suaeda vermiculata for Antioxidant and Cytotoxic Activities

Molecules ◽  
2019 ◽  
Vol 24 (8) ◽  
pp. 1501 ◽  
Author(s):  
Hamdoon A. Mohammed ◽  
Mohsen S. Al-Omar ◽  
Mahmoud Zaki El-Readi ◽  
Ahmad H. Alhowail ◽  
Maha A. Aldubayan ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Ascorbic Acid ◽  
Ethyl Cellulose ◽  
Cytotoxic Effect ◽  
Reducing Power ◽  
Chloroform Extract ◽  
Water Soluble ◽  
Pheophytin A ◽  
Wide Range ◽  
Mcf 7

Background: This study is designed to discover a method for delivering an efficient potent pheophytin a (pheo-a) into more absorbed and small polymeric ethyl cellulose (EC) microparticles. Methods: Silica gel and Sephadex LH-20 columns were used to isolate pheo-a from the chloroform extract of the edible plant, Suaeda vermiculata. Pheo-a was incorporated into EC microparticles using emulsion-solvent techniques. The antioxidant activity of pheo-a microparticles was confirmed by the level of superoxide radical (SOD), nitric oxide (NO), and reducing power (RP) methods. Meanwhile, the cytotoxic effect of the product was investigated on MCF-7 cells using MTT assay. Results: Pheo-a was isolated from S. vermiculata in a 12% concentration of the total chloroform extract. The structures were confirmed by NMR and IR spectroscopic analysis. The formulated microparticles were uniform, completely dispersed in the aqueous media, compatible as ingredients, and had a mean diameter of 139 ± 1.56 µm as measured by a particle size analyzer. Pheo-a demonstrated a valuable antioxidant activity when compared with ascorbic acid. The IC50 values of pheo-a microparticles were 200.5 and 137.7 µg/mL for SOD, and NO respectively. The reducing power of pheo-a microparticles was more potent than ascorbic acid and had a 4.2 µg/mL for IC50 value. Pheo-a microparticles did not show notable cytotoxicity on the MCF-7 cell line (IC50 = 35.9 µg/mL) compared with doxorubicin (IC50 = 3.2 µg/mL). Conclusions: the results showed that water-soluble pheo-a microparticles were prepared with a valuable antioxidant activity in a wide range of concentrations with a noteworthy cytotoxic effect.

scholarly journals Antioxidant Peptides from the Protein Hydrolysate of Spanish Mackerel (Scomberomorous niphonius) Muscle by in Vitro Gastrointestinal Digestion and Their in Vitro Activities

Marine Drugs ◽  
2019 ◽  
Vol 17 (9) ◽  
pp. 531 ◽  
Author(s):  
Zhao ◽  
Yang ◽  
Wang ◽  
Zhao ◽  
Chi ◽  
...  
Keyword(s):  
Protein Hydrolysate ◽  
Radical Scavenging ◽  
Model Systems ◽  
Dpph Radical ◽  
Antioxidant Peptides ◽  
Gastrointestinal Digestion ◽  
Spanish Mackerel ◽  
In Vitro Gastrointestinal Digestion ◽  
Dpph Radical Scavenging

For the full use of Spanish mackerel (Scomberomorous niphonius) muscle to produce antioxidant peptides, the proteins of Spanish mackerel muscle were separately hydrolyzed under five kinds of enzymes and in vitro gastrointestinal digestion, and antioxidant peptides were isolated from the protein hydrolysate using ultrafiltration and multiple chromatography methods. The results showed that the hydrolysate (SMPH) prepared using in vitro GI digestion showed the highest degree of hydrolysis (27.45 ± 1.76%) and DPPH radical scavenging activity (52.58 ± 2.68%) at the concentration of 10 mg protein/mL among the six protein hydrolysates, and 12 peptides (SMP-1 to SMP-12) were prepared from SMPH. Among them, SMP-3, SMP-7, SMP-10, and SMP-11 showed the higher DPPH radical scavenging activities and were identified as Pro-Glu-Leu-Asp-Trp (PELDW), Trp-Pro-Asp-His-Trp (WPDHW), and Phe-Gly-Tyr-Asp-Trp-Trp (FGYDWW), and Tyr-Leu-His-Phe-Trp (YLHFW), respectively. PELDW, WPDHW, FGYDWW, and YLHFW showed high scavenging activities on DPPH radical (EC50 1.53, 0.70, 0.53, and 0.97 mg/mL, respectively), hydroxyl radical (EC50 1.12, 0.38, 0.26, and 0.67 mg/mL, respectively), and superoxide anion radical (EC50 0.85, 0.49, 0.34, and 1.37 mg/mL, respectively). Moreover, PELDW, WPDHW, FGYDWW, and YLHFW could dose-dependently inhibit lipid peroxidation in the linoleic acid model system and protect plasmid DNA (pBR322DNA) against oxidative damage induced by H2O2 in the tested model systems. In addition, PELDW, WPDHW, FGYDWW, and YLHFW could retain their high activities when they were treated under a low temperature (<60 °C) and a moderate pH environment (pH 5–9). These present results indicate that the protein hydrolysate, fractions, and isolated peptides from Spanish mackerel muscle have strong antioxidant activity and might have the potential to be used in health food products.

scholarly journals Purification and Identification of Antioxidant Alcalase-Derived Peptides from Sheep Plasma Proteins

Antioxidants ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 592 ◽  
Author(s):  
Chengli Hou ◽  
Liguo Wu ◽  
Zhenyu Wang ◽  
Elena Saguer ◽  
Dequan Zhang
Keyword(s):  
Liquid Chromatography ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Amino Acid Sequences ◽  
Dpph Radical ◽  
Antioxidant Peptides ◽  
Animal Blood ◽  
Antioxidant Power ◽  
Radical Scavenging Ability ◽  
Dpph Radical Scavenging

In this study, sheep plasma was submitted to Alcalase-hydrolysis and peptides with better antioxidant properties measured through both the ferric-reducing antioxidant power (FRAP) and the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging ability assays were isolated and identified. After hydrolysate ultrafiltration and semi-preparative reverse-phase high-performance liquid chromatography, nine fractions (F1–F9) were obtained, with the two first (F1 and F2) showing the greatest antioxidant potential. These two fractions were further separated by the AKTA purifier system to generate four (F1-1–F1-4) and five (F2-1–F2-5) fractions, respectively, with two of them (F1-2 and F2-1) exhibiting appreciable FRAP activity and DPPH radical scavenging ability. Using liquid chromatography-tandem mass spectrometry, three antioxidant peptides were identified. From their amino acid sequences (QTALVELLK, SLHTLFGDELCK, and MPCTEDYLSLILNR), which include amino acids that have been previously reported as key contributors to the peptide antioxidant properties, it can be maintained that they come mainly from serum albumin. These results suggested that the sheep plasma protein can be considered as a good source of antioxidant peptides and bring forth new possibilities for the utilization of animal blood by-products.

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