scholarly journals Effects of Germination on Protein, γ-Aminobutyric Acid, Phenolic Acids, and Antioxidant Capacity in Wheat

Molecules ◽  
2018 ◽  
Vol 23 (9) ◽  
pp. 2244 ◽  
Author(s):  
Mi Kim ◽  
Han Kwak ◽  
Sang Kim
Keyword(s):  
Antioxidant Capacity ◽  
Phenolic Acids ◽  
Antioxidant Properties ◽  
Peptide Mass Fingerprinting ◽  
Aminobutyric Acid ◽  
Food Material ◽  
Two Dimensional Gel Electrophoresis ◽  
Potential Health ◽  
Peptide Mass ◽  
Close Relationship

Germinated wheat is a food material with potential health benefits due to its high phenolic and antioxidant content, but the reason why germination increases this content is unclear. The aim of this study was to investigate the relationships between protein changes (determined by two-dimensional gel electrophoresis (2-DE)), phenolics, γ-aminobutyric acid (GABA) levels, and antioxidant capacity of wheat germinated for various periods (24, 48, 72, and 96 h) compared to control. Each phenolic acid tended to increase with increasing germination time. The GABA content was highest (39.98 mg/100 g dwb) after 96 h of germination. The total oxygen radical absorbance capacity (ORAC) was 1.97 times higher after 96 h than in ungerminated seeds. Fifteen proteins, among 82 proteins separated by 2-DE, were highly related with ORAC and were identified by peptide mass fingerprinting (PMS). The PMS revealed strong expression of granule bound starch synthase (GBSS) and glutathione S-transferase (GSTF) after 96 h of germination. Overall, the ORAC at 96 h exhibited a close relationship with the levels of phenolic acids, GABA, and proteins such as GBSS and GSTF. In conclusion, these findings add to the existing knowledge of wheat protein changes and their relationship to the antioxidant properties of germinating wheat seeds.

scholarly journals Screening and Characterization of Phenolic Compounds and Their Antioxidant Capacity in Different Fruit Peels

Foods ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1206 ◽  
Author(s):  
Hafiz A. R. Suleria ◽  
Colin J. Barrow ◽  
Frank R. Dunshea
Keyword(s):  
Phenolic Compounds ◽  
Antioxidant Capacity ◽  
Phenolic Acids ◽  
Phenolic Content ◽  
Antioxidant Properties ◽  
Antioxidant Potential ◽  
Fruit Peel ◽  
Diverse Range ◽  
Mango Peel

Fruit peels have a diverse range of phytochemicals including carotenoids, vitamins, dietary fibres, and phenolic compounds, some with remarkable antioxidant properties. Nevertheless, the comprehensive screening and characterization of the complex array of phenolic compounds in different fruit peels is limited. This study aimed to determine the polyphenol content and their antioxidant potential in twenty different fruit peel samples in an ethanolic extraction, including their comprehensive characterization and quantification using the LC-MS/MS and HPLC. The obtained results showed that the mango peel exhibited the highest phenolic content for TPC (27.51 ± 0.63 mg GAE/g) and TFC (1.75 ± 0.08 mg QE/g), while the TTC (9.01 ± 0.20 mg CE/g) was slightly higher in the avocado peel than mango peel (8.99 ± 0.13 mg CE/g). In terms of antioxidant potential, the grapefruit peel had the highest radical scavenging capacities for the DPPH (9.17 ± 0.19 mg AAE/g), ABTS (10.79 ± 0.56 mg AAE/g), ferric reducing capacity in FRAP (9.22 ± 0.25 mg AA/g), and total antioxidant capacity, TAC (8.77 ± 0.34 mg AAE/g) compared to other fruit peel samples. The application of LC-ESI-QTOF-MS/MS tentatively identified and characterized a total of 176 phenolics, including phenolic acids (49), flavonoids (86), lignans (11), stilbene (5) and other polyphenols (25) in all twenty peel samples. From HPLC-PDA quantification, the mango peel sample showed significantly higher phenolic content, particularly for phenolic acids (gallic acid, 14.5 ± 0.4 mg/g) and flavonoids (quercetin, 11.9 ± 0.4 mg/g), as compared to other fruit peel samples. These results highlight the importance of fruit peels as a potential source of polyphenols. This study provides supportive information for the utilization of different phenolic rich fruit peels as ingredients in food, feed, and nutraceutical products.

scholarly journals Altered Protein Expression of Streptococcus oralis Cultured at Low pH Revealed by Two-Dimensional Gel Electrophoresis

2001 ◽  
Vol 67 (8) ◽  
pp. 3396-3405 ◽  
Author(s):  
Joanna C. Wilkins ◽  
Karen A. Homer ◽  
David Beighton
Keyword(s):  
Gel Electrophoresis ◽  
Peptide Mass Fingerprinting ◽  
Low Ph ◽  
Ionization Mass ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Altered Expression ◽  
Streptococcus Oralis ◽  
Peptide Mass

ABSTRACT Streptococcus oralis is the predominant aciduric nonmutans streptococcus isolated from the human dentition, but the role of this organism in the initiation and progression of dental caries has yet to be established. To identify proteins that are differentially expressed by S. oralis growing under conditions of low pH, soluble cellular proteins extracted from bacteria grown in batch culture at pH 5.2 or 7.0 were analyzed by two-dimensional (2-D) gel electrophoresis. Thirty-nine proteins had altered expression at low pH; these were excised, digested with trypsin using an in-gel protocol, and further analyzed by peptide mass fingerprinting using matrix-assisted laser desorption ionization mass spectrometry. The resulting fingerprints were compared with the genomic database forStreptococcus pneumoniae, an organism that is phylogenetically closely related to S. oralis, and putative functions for the majority of these proteins were determined on the basis of functional homology. Twenty-eight proteins were up-regulated following growth at pH 5.2; these included enzymes of the glycolytic pathway (glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase), the polypeptide chains comprising ATP synthase, and proteins that are considered to play a role in the general stress response of bacteria, including the 60-kDa chaperone, Hsp33, and superoxide dismutase, and three distinct ABC transporters. These data identify, for the first time, gene products that may be important in the survival and proliferation of nonmutans aciduric S. oralis under conditions of low pH that are likely to be encountered by this organism in vivo.

Proteomic analysis of multiple sclerosis cerebrospinal fluid

2004 ◽  
Vol 10 (3) ◽  
pp. 245-260 ◽  
Author(s):  
B N Hammack ◽  
K YC Fung ◽  
S W Hunsucker ◽  
M W Duncan ◽  
M P Burgoon ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Cerebrospinal Fluid ◽  
Calcium Binding ◽  
Cell Signalling ◽  
Protein A ◽  
Peptide Mass Fingerprinting ◽  
Two Dimensional Gel Electrophoresis ◽  
Ph Gradients ◽  
Peptide Mass ◽  
Normal Human

Two-dimensional gel electrophoresis and peptide mass fingerprinting were used to identify proteins in cerebrospinal fluid (C SF) pooled from three patients with multiple sclerosis (MS) and in C SF pooled from three patients with non-MS inflammatory central nervous system (C NS) disorders. Resolution of C SF proteins on three pH gradients (3-10, 4-7 and 6-11) enabled identification of a total of 430 spots in the MS C SF proteome that represented 61 distinct proteins. The gels containing MS C SF revealed 103 protein spots that were not seen on control gels. A ll but four of these 103 spots were proteins known to be present in normal human C SF. The four exceptio ns were: C RTAC -1B (cartilage acidic protein), tetranectin (a plasminogen-binding protein), SPARC -like protein (a calcium binding cell signalling glycoprotein), and autotaxin t (a phosphodiesterase). It remains unknown whether these four proteins are related to the cause and patho genesis of MS.

scholarly journals Hyperoxia-Induced Protein Alterations in Renal Rat Tissue: A Quantitative Proteomic Approach to Identify Hyperoxia-Induced Effects in Cellular Signaling Pathways

2015 ◽  
Vol 2015 ◽  
pp. 1-12 ◽  
Author(s):  
Jochen Hinkelbein ◽  
Lennert Böhm ◽  
Oliver Spelten ◽  
David Sander ◽  
Stefan Soltész ◽  
...  
Keyword(s):  
Protein Expression ◽  
Rat Kidney ◽  
Peptide Mass Fingerprinting ◽  
Renal Tissue ◽  
Short Term ◽  
Two Dimensional Gel Electrophoresis ◽  
Normobaric Hyperoxia ◽  
Peptide Mass ◽  
Proteomic Approach ◽  
Hyperoxia Exposure

Introduction. In renal tissue as well as in other organs, supranormal oxygen pressure may lead to deleterious consequences on a cellular level. Additionally, hyperoxia-induced effect in cells and related free radicals may potentially contribute to renal failure. The aim of this study was to analyze time-dependent alterations of rat kidney protein expression after short-term normobaric hyperoxia using proteomics and bioinformatic approaches.Material and Methods.N=36Wistar rats were randomized into six different groups: three groups with normobaric hyperoxia (exposure to 100% oxygen for 3 h) and three groups with normobaric normoxia (NN; room air). After hyperoxia exposure, kidneys were removed immediately, after 3 days and after 7 days. Kidney lysates were analyzed by two-dimensional gel electrophoresis followed by peptide mass fingerprinting using tandem mass spectrometry. Statistical analysis was performed with DeCyder 2D software (p<0.01). Biological functions of differential regulated proteins were studied using functional network analysis (Ingenuity Pathways Analysis and PathwayStudio).Results. Expression of 14 proteins was significantly altered(p<0.01): eight proteins (MEP1A_RAT, RSSA_RAT, F16P1_RAT, STML2_RAT, BPNT1_RAT, LGMN_RAT, ATPA_RAT, and VDAC1_RAT) were downregulated and six proteins (MTUS1_RAT, F16P1_RAT, ACTG_RAT, ACTB_RAT, 2ABA_RAT, and RAB1A_RAT) were upregulated. Bioinformatic analyses revealed an association of regulated proteins with inflammation.Conclusions. Significant alterations in renal protein expression could be demonstrated for up to 7 days even after short-term hyperoxia. The identified proteins indicate an association with inflammation signaling cascades. MEP1A and VDAC1 could be promising candidates to identify hyperoxic injury in kidney cells.

Proteomic analysis defines altered cellular redox pathways and advanced glycation end-product metabolism in glomeruli of db/db diabetic mice

2007 ◽  
Vol 293 (4) ◽  
pp. F1157-F1165 ◽  
Author(s):  
Michelle T. Barati ◽  
Michael L. Merchant ◽  
Angela B. Kain ◽  
Anthony W. Jevans ◽  
Kenneth R. McLeish ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Proteomic Analysis ◽  
Adaptive Response ◽  
Renal Cortex ◽  
Peptide Mass Fingerprinting ◽  
Glyoxalase I ◽  
Diabetic Mice ◽  
Two Dimensional Gel Electrophoresis ◽  
Peptide Mass

To attain a profile of protein expression during diabetes, we applied proteomic analysis to glomeruli of 160-day-old db/db diabetic and db/m nondiabetic mice. Glomerular proteins were extracted and separated by two-dimensional gel electrophoresis to construct a proteome map. Matrix-assisted laser desorption and ionization-time of flight mass spectrometry and peptide mass fingerprinting were used to identify 190 proteins. Of 105 analyzed spots, expression of 40 proteins, including the antioxidative enzymes peroxiredoxin 1 and 3, glutathione peroxidase 1, and SOD-1, was increased with diabetes, suggesting an adaptive response to oxidative stress associated with this diabetic model. However, activity of glutathione peroxidase and SOD was unaltered in glomeruli of diabetic mice. Expression of glyoxalase I was increased in glomeruli of diabetic mice. Because the cofactor for glyoxalase I, glutathione, is decreased in renal cortex of db/db mice, renal cortical glyoxalase I activity was measured in vitro with fixed amounts of exogenous glutathione. Glyoxalase I activity was decreased in renal cortex of db/db mice. These data indicate that diabetes-induced decreases in glyoxalase I activity are likely to be due to glutathione-dependent and -independent mechanisms and that increased expression of glyoxalase I may represent an insufficient adaptive response to increased methylglyoxal formation.

scholarly journals Impact of Cold versus Hot Brewing on the Phenolic Profile and Antioxidant Capacity of Rooibos (Aspalathus linearis) Herbal Tea

Antioxidants ◽  
2019 ◽  
Vol 8 (10) ◽  
pp. 499 ◽  
Author(s):  
Elisabetta Damiani ◽  
Patricia Carloni ◽  
Gabriele Rocchetti ◽  
Biancamaria Senizza ◽  
Luca Tiano ◽  
...  
Keyword(s):  
Antioxidant Capacity ◽  
Phenolic Acids ◽  
Polyphenol Content ◽  
Herbal Tea ◽  
Potential Health ◽  
Phenolic Profile ◽  
Aspalathus Linearis ◽  
Antioxidant Capacities ◽  
The Impact

Consumption of rooibos (Aspalathus linearis) as herbal tea is growing in popularity worldwide and its health-promoting attributes are mainly ascribed to its phenolic composition, which may be affected by the brewing conditions used. An aspect so far overlooked is the impact of cold brewing vs regular brewing and microwave boiling on the (poly) phenolic profile and in vitro antioxidant capacity of infusions prepared from red (‘fermented’, oxidized) and green (‘unfermented’, unoxidized) rooibos, the purpose of the present study. By using an untargeted metabolomics-based approach (UHPLC-QTOF mass spectrometry), 187 phenolic compounds were putatively annotated in both rooibos types, with flavonoids, tyrosols, and phenolic acids the most represented type of phenolic classes. Multivariate statistics (OPLS-DA) highlighted the phenolic classes most affected by the brewing conditions. Similar antioxidant capacities (ORAC and ABTS assays) were observed between cold- and regular-brewed green rooibos and boiled-brewed red rooibos. However, boiling green and red rooibos delivered infusions with the highest antioxidant capacities and total polyphenol content. The polyphenol content strongly correlated with the in vitro antioxidant capacities, especially for flavonoids and phenolic acids. These results contribute to a better understanding of the impact of the preparation method on the potential health benefits of rooibos tea.

Comparative proteome analysis of drought-sensitive and drought-tolerant maize leaves under osmotic stress

2019 ◽  
Vol 99 (4) ◽  
pp. 467-479
Author(s):  
Yuhe Pei ◽  
Jianfen Bai ◽  
Xinmei Guo ◽  
Meiai Zhao ◽  
Qingmei Ma ◽  
...  
Keyword(s):  
Osmotic Stress ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Inbred Lines ◽  
Limiting Factor ◽  
Two Dimensional Gel Electrophoresis ◽  
Maize Production ◽  
Drought Tolerant ◽  
Maize Inbred Lines ◽  
Peptide Mass

Drought is a major yield-limiting factor in maize production. Osmotic stress was applied to two maize inbred lines with polyethylene glycol 6000 treatments. Proteins from the leaves were analyzed by two-dimensional gel electrophoresis and peptide mass fingerprinting at two time points, 24 and 48 h after osmotic stress. Thirty-five proteins were differentially expressed between control and treatment groups in the two maize inbred lines. In ‘Qi319’, a drought-tolerant inbred line, there were five up-regulated proteins at 24 h and 13 up-regulated and one down-regulated protein at 48 h. In drought-sensitive line ‘Zheng58’, 10 proteins were up-regulated at 24 h, while six proteins were up-regulated at 48 h. The 35 proteins were subjected to mass spectrometry and 17 proteins were successfully identified. These proteins were classified into six categories: photosynthesis-related, energy and metabolism, signaling pathways, protein synthesis, defense-related, and unclassified.

scholarly journals Identification of Streptomyces coelicolor Proteins That Are Differentially Expressed in the Presence of Plant Material

2003 ◽  
Vol 69 (4) ◽  
pp. 1884-1889 ◽  
Author(s):  
P. Langlois ◽  
S. Bourassa ◽  
G. G. Poirier ◽  
C. Beaulieu
Keyword(s):  
Plant Material ◽  
Lemna Minor ◽  
Streptomyces Coelicolor ◽  
Carbon Sources ◽  
Peptide Mass Fingerprinting ◽  
Pentose Phosphate ◽  
Stress Conditions ◽  
Two Dimensional Gel Electrophoresis ◽  
Bacterial Gene ◽  
Peptide Mass

ABSTRACT Streptomyces coelicolor and Lemna minor were used as a model to study the modulation of bacterial gene expression during plant-streptomycete interactions. S. coelicolor was grown in minimal medium with and without L. minor fronds. Bacterial proteomes were analyzed by two-dimensional gel electrophoresis, and a comparison of the two culture conditions resulted in identification of 31 proteins that were induced or repressed by the presence of plant material. One-half of these proteins were identified by peptide mass fingerprinting by using matrix-assisted laser desorption ionization-time of flight mass spectrometry. The induced proteins were involved in energetic metabolism (glycolysis, pentose phosphate pathway, oxidative phosphorylation), protein synthesis, degradation of amino acids, alkenes, or cellulose, tellurite resistance, and growth under general physiological or oxidative stress conditions. The repressed proteins were proteins synthesized under starvation stress conditions. These results suggest that root exudates provide additional carbon sources to the bacteria and that physiological adaptations are required for efficient bacterial growth in the presence of plants.

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