scholarly journals Effect of Low-Frequency Ultrasonic-Assisted Enzymolysis on the Physicochemical and Antioxidant Properties of Corn Protein Hydrolysates

2017 ◽  
Vol 2017 ◽  
pp. 1-10 ◽  
Author(s):  
Qiufang Liang ◽  
Xiaofeng Ren ◽  
Haile Ma ◽  
Suyun Li ◽  
Kangkang Xu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Orthogonal Design ◽  
Protein A ◽  
Antioxidant Properties ◽  
Low Frequency ◽  
Antioxidant Peptides ◽  
Corn Protein ◽  
Ultrasonic Assisted ◽  
Pretreatment Conditions ◽  
Ultrasound Pretreatment

The aim of this study was to investigate the effect of low-frequency ultrasound on the enzymolysis of corn protein. A L9(34) orthogonal design was used to optimize ultrasound pretreatment conditions. Degree hydrolysis (DH), conversion rate of protein (CR), and DPPH IC50were selected as analytical indicators. Under the optimal ultrasound conditions (5 W/L power, 2 s/2 s on/off time, 50°C temperature, and 25 min time), the DH, CR, and radical (DPPH∙,OH∙) scavenging capacities were significantly increased. Molecular weight distribution and amino acid profile analysis showed that ultrasound pretreatment enhanced the formation of short-chain peptides with molecular weight of 200–3000 Da, especially the peptides containing hydrophobic amino acids. Moreover, 40 potential antioxidant peptides were purified by C18 semipreparative column and identified by UPLC-ESI-MS. The results suggest that the optimal ultrasonic-assisted enzymolysis technology could be useful for preparation of antioxidant peptides from corn.

scholarly journals Antioxidant properties and inhibition of angiotensin-converting enzyme by highly active peptides from wheat gluten

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Wen-Ying Liu ◽  
Jiang-Tao Zhang ◽  
Takuya Miyakawa ◽  
Guo-Ming Li ◽  
Rui-Zeng Gu ◽  
...  
Keyword(s):  
Wheat Gluten ◽  
Antioxidant Properties ◽  
Converting Enzyme ◽  
Antioxidant Peptides ◽  
Active Peptides ◽  
Inhibitory Peptides ◽  
Highly Active ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

AbstractThis study aimed to focus on the high-value utilization of raw wheat gluten by determining the potent antioxidant peptides and angiotensin I-converting enzyme (ACE) inhibitory peptides from wheat gluten oligopeptides (WOP). WOP were analyzed for in vitro antioxidant activity and inhibition of ACE, and the identification of active peptides was performed by reversed-phase high-performance liquid chromatography and mass spectrometry. Quantitative analysis was performed for highly active peptides. Five potent antioxidant peptides, Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (6.07 ± 0.38, 7.28 ± 0.29, 11.18 ± 1.02, 5.93 ± 0.20 and 9.04 ± 0.47 mmol 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid (Trolox) equivalent/g sample, respectively), and five potent ACE inhibitory peptides, Leu-Tyr, Leu-Val-Ser, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (half maximal inhibitory concentration (IC50) values = 0.31 ± 0.02, 0.60 ± 0.03, 2.00 ± 0.13, 1.47 ± 0.08 and 1.48 ± 0.11 mmol/L, respectively), were observed. The contents of Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser were 155.04 ± 8.36, 2.08 ± 0.12, 1.95 ± 0.06, 22.70 ± 1.35, 0.25 ± 0.01, and 53.01 ± 2.73 μg/g, respectively, in the WOP. Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser are novel antioxidative/ACE inhibitory peptides that have not been previously reported. The results suggest that WOP could potentially be applied in the food industry as a functional additive.

Antioxidant peptides from corn gluten meal: Orthogonal design evaluation

2015 ◽  
Vol 187 ◽  
pp. 270-278 ◽  
Author(s):  
Cunshan Zhou ◽  
Jiali Hu ◽  
Haile Ma ◽  
Abu ElGasim A. Yagoub ◽  
Xiaojie Yu ◽  
...  
Keyword(s):  
Orthogonal Design ◽  
Design Evaluation ◽  
Antioxidant Peptides ◽  
Corn Gluten Meal ◽  
Corn Gluten

scholarly journals Studies on human pregnancy-associated plasma protein A. Purification by affinity chromatography and structural comparisons with α2-macroglobulin

1980 ◽  
Vol 191 (3) ◽  
pp. 799-809 ◽  
Author(s):  
R G Sutcliffe ◽  
B M Kukulska-Langlands ◽  
J R Coggins ◽  
J B Hunter ◽  
C H Gore
Keyword(s):  
Molecular Weight ◽  
Affinity Chromatography ◽  
Plasma Protein ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Carbohydrate Content ◽  
Polyacrylamide Gel ◽  
Gel Chromatography ◽  
Tryptic Fragment

Pregnancy-associated plasma protein-A (PAPP-A) has been purified by a combination of methods including antibody-affinity chromatography. The resultant protein, obtained in 16% yield from maternal serum, appeared as a single major component on non-denaturing polyacrylamide and SDS/polyacrylamide gel electrophoresis. The protein showed a single component when analysed by isoelectric focusing under denaturing conditions in the presence and absence of reduction and had a pI of 4.34 and 4.42 respectively. These pI values were indistinguishable from those of alpha 2-macroglobulin (alpha 2M). The molecular weight of the PAPP-A polypeptide as shown by SDS/polyacrylamide-gel electrophoresis was 187000, with a minor component of mol.wt. 82500 that was attributed to proteolysis. Since native PAPP-A had a molecular weight on gel chromatography very similar to that of alpha 2M (620000–820000), it was concluded that PAPP-A was a homotetramer. In the absence of reduction, a high-molecular-weight (420000) protomer of PAPP-A was found. It was deduced that PAPP-A, like alpha 2M, is a dinner, whose protomers are composed of disulphide-linked polypeptide chains. It was found that the molecular weight of the PAPP-A polypeptide exceeded that of alpha 2M by 3.3%, but that the total carbohydrate content of PAPP-A exceeded that of alpha 2M by 10% and that its neutral carbohydrate content exceeded that of alpha 2M by between 7.4 and 9.0%. The significance of the estimated molecular weights of alpha 2M (181000) and its major tryptic fragments is discussed in the light of published values. A tryptic fragment alpha 2M (82500 mol.wt.) was apparently the same size as the major tryptic fragment of PAPP-A.

scholarly journals Physicochemical and Antioxidant Properties of the Degradations of Polysaccharides from Dendrobium officinale and Their Suitable Molecular Weight Range on Inducing HeLa Cell Apoptosis

2019 ◽  
Vol 2019 ◽  
pp. 1-11 ◽  
Author(s):  
Xiaofeng Zhang ◽  
Yingyi Luo ◽  
Gang Wei ◽  
Yunrong Li ◽  
Yuechun Huang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Antitumor Activity ◽  
Hela Cells ◽  
Biological Activities ◽  
Antioxidant Properties ◽  
Mitochondrial Pathway ◽  
Influential Factor ◽  
Dendrobium Officinale ◽  
Molecular Weight Range ◽  
Pharmaceutical Industries

Different molecular weight polysaccharides of Dendrobium officinale (DOPs) have gradually attracted attention because of their broad biological activities. They, however, remain poorly defined whether their antitumor activity is associated with molecular weight. In this study, the physicochemical, antioxidant, and antitumor properties of DOPs, including the crude polysaccharide (DOP) and its six degradation fractions (DOP1–DOP6) extracted from Dendrobium officinale, were determined. Consequently, DOPs were mainly composed of different ratios of mannose and glucose as follows: 5.15 : 1, 4.62 : 1, 4.19 : 1, 4.46 : 1, 4.32 : 1, 4.29 : 1, and 4.23 : 1, and their molecular weights were significantly different ranging from 652.29 kDa to 11.10 kDa. With the concentration increase of DOPs, the scavenging capacity against OH and DPPH free radicals increased. The antitumor ability of DOPs was different that DOP1–DOP5 (Mw: 176.29 kDa–28.48 kDa) exhibited the best antiproliferation activity than DOP (Mw: 652.29 kDa) and DOP6 (Mw: 11.10 kDa) in HeLa cells rather than PC9, A549, and HepG2 cells. Moreover, it is worth mentioning that DOP1 and DOP5 showed stronger capability on inducing apoptosis of HeLa cells than DOP and DOP6 via the mitochondrial pathway by upregulating the ratio of the Bax/Bal-2 mRNA expression. The results demonstrated that DOPs can be used as the potential natural antioxidant and antitumor products in pharmaceutical industries, and the molecular weight is a crucial influential factor of their antitumor activity that 28.48 kDa–176.29 kDa is a suitable range we may refer to.

scholarly journals In Vitro Antioxidant Activity and FTIR Characterization of High-Molecular Weight Melanoidin Fractions from Different Types of Cocoa Beans

Antioxidants ◽  
2019 ◽  
Vol 8 (11) ◽  
pp. 560 ◽  
Author(s):  
Oracz ◽  
Zyzelewicz
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Antioxidant Properties ◽  
Model Systems ◽  
Total Phenolic ◽  
Cocoa Beans ◽  
Potential Health ◽  
Antioxidant Power ◽  
Different Types

Melanoidins from real foods and model systems have received considerable interest due to potential health benefits. However, due to the complexity of these compounds, to date, the exact structure of melanoidins and mechanism involved in their biological activity has not been fully elucidated. Thus, the aim of this study was to investigate the total phenolic content, antioxidant properties, and structural characteristics of high-molecular weight (HMW) melanoidin fractions isolated by dialysis (>12.4 kDa) from raw and roasted cocoa beans of Criollo, Forastero, and Trinitario beans cultivated in various area. In vitro antioxidant properties of all studied HMW cocoa fractions were evaluated by four different assays, namely free radical scavenging activity against DPPH● and ABTS●+ radicals, ferric reducing antioxidant power (FRAP), and metal-chelating ability. Additionally, the structure–activity relationship of isolated HMW melanoidin fractions were analyzed using attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). The results show that roasting at a temperature of 150 °C and a relative air humidity of 0.3% effectively enhances the total phenolics content and the antioxidant potential of almost all HMW cocoa melanoidin fractions. The ATR-FTIR analysis revealed that the various mechanisms of action of HMW melanoidins isolates of different types of cocoa beans related to their structural diversity. Consequently, the results clearly demonstrated that HMW cocoa fractions isolated from cocoa beans (especially those of Criollo variety) roasted at higher temperatures with the lower relative humidity of air possess high antioxidant properties in vitro.

scholarly journals PADGEM protein in human erythroleukemia cells

Blood ◽  
1989 ◽  
Vol 73 (3) ◽  
pp. 722-728 ◽  
Author(s):  
E Yeo ◽  
BC Furie ◽  
B Furie
Keyword(s):  
Molecular Weight ◽  
Binding Sites ◽  
Protein A ◽  
Flow Cytometric Analysis ◽  
Surface Expression ◽  
Membrane Glycoproteins ◽  
Surface Binding ◽  
Cell Content ◽  
Granule Membrane ◽  
Hel Cells

Abstract PADGEM protein, a platelet alpha granule membrane glycoprotein with a molecular weight of 140,000, is translocated to the plasma membrane during granule secretion and platelet activation. PADGEM protein is expressed on the surface of activated platelets but not on the surface of resting platelets. Human erythroleukemia (HEL) cells contain platelet alpha granule-like organelles, alpha granule proteins, and express platelet membrane glycoproteins GPIIb/IIIa and GPIb. We demonstrate that HEL cells express a protein that has a molecular weight identical to that of PADGEM and binds to anti-PADGEM antibodies. The exposure of HEL cells in culture to dimethylsulfoxide (DMSO) increased the number of cells expressing PADGEM. Fluorescence activated flow cytometric analysis demonstrated an increase in mean surface expression of PADGEM in DMSO-exposed cells compared to noninduced cells. Total cell content of PADGEM was increased 5.3-fold after DMSO exposure, as determined by radioimmunoassay. Direct binding experiments with the monoclonal anti-PADGEM antibody KC4 demonstrated specific, saturable, and time-dependent interaction of KC4 with HEL cells. A Kd of 7 nM was estimated. There were 14,000 surface binding sites per cell in noninduced cells and 24,000 surface binding sites per cell in DMSO- induced HEL cells. Surface expression of PADGEM protein on HEL cells was not increased with platelet agonists, including thrombin, epinephrine, ADP, nor cytokines, including IL-1, IL-2, tissue necrosis factor. The presence of PADGEM protein in HEL cells should facilitate the elucidation of the function of PADGEM protein.

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.

Sign in / Sign up

Export Citation Format

Share Document