HPLC–ESI-Q-TOF-MS for a comprehensive characterization of bioactive phenolic compounds in cucumber whole fruit extract

Abu‐Reidah, Ibrahim M.; Arráez‐Román, David; Quirantes-Piné, Rosa; Fernández-Arroyo, Salvador; Segura‐Carretero, Antonio; Fernández‐Gutiérrez, Alberto

doi:10.1016/j.foodres.2011.11.026

Cited by 118 publications

(79 citation statements)

References 40 publications

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“…The relative molecular mass of the purified protein was confirmed using SDS‐PAGE and electrospray ionization quadrupole time‐of‐flight mass spectrometry / mass spectrometry (ESI Q‐TOF MS/MS) according to a previous method (Abu‐Reidah and others ). Analysis of the N‐terminal amino acid sequence of the purified protein was identified by Edman degradation using a ABI 492 Procise Protein Seuqencer (Perkin‐Elmer Corp., Applied Biosystems Division, Foster City, CA, USA).…”

Section: Methodsmentioning

confidence: 99%

Antioxidant Activity of Oxygen Evolving Enhancer Protein 1 Purified from Capsosiphon fulvescens

Kim

Choi

Lee

et al. 2015

Journal of Food Science

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This study was conducted to determine the antioxidant activity of a protein purified from Capsosiphon fulvescens. The purification steps included sodium acetate (pH 6) extraction and diethylaminoethyl-cellulose, reversed phase Shodex C4P-50 column chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis indicated that the molecular weight of the purified protein was 33 kDa. The N-terminus and partial peptide amino acid sequence of this protein was identical to the sequence of oxygen evolving enhancer (OEE) 1 protein. The antioxidant activity of the OEE 1 was determined in vitro using a scavenging test with 4 types of reactive oxygen species (ROS), including the 2,2-diphenyl-1-picrylhydrazyl radical, hydroxyl radical, superoxide anion, and hydrogen peroxide (H2 O2 ). OEE 1 had higher H2 O2 scavenging activity, which proved to be the result of enzymatic antioxidants rather than nonenzymatic antioxidants. In addition, OEE 1 showed less H2 O2 -mediated ROS formation in HepG2 cells. In conclusion, this study demonstrates that OEE 1 purified from C. fulvescens is an excellent antioxidant.

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Section: Methodsmentioning

confidence: 99%

Antioxidant Activity of Oxygen Evolving Enhancer Protein 1 Purified from Capsosiphon fulvescens

Kim

Choi

Lee

et al. 2015

Journal of Food Science

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show abstract

“…Analysis of protein expression and purification were carried out using sodium dodecyl sulfate -poly acrylamide gel electrophoresis (SDS-PAGE). The purified recombinant PPI protein was confirmed using SDS-PAGE and electrospray ionization quadrupole time-of-flight mass spectrometry/mass spectrometry (ESI-Q-TOF MS/MS), according to a previously described method (32). The proteins were identified via an NCBI search using the MASCOT program (, Matrixscience, London, UK).…”

Section: Methodsmentioning

confidence: 99%

Effects of the cyclophilin-type peptidylprolyl cis-trans isomerase from Pyropia yezoensis against hydrogen peroxide-induced oxidative stress in HepG2 cells

Kim

Choi

et al. 2017

Molecular Medicine Reports

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The present study aimed to describe the expression and purification of cyclophilin-type peptidylprolyl cis-trans isomerase (PPI) from the red alga Pyropia yezoensis. The antioxidant activity of the purified protein was also demonstrated, based on its ability to act against oxidative stress in HepG2 human hepatocellular carcinoma cells. HepG2 cells that were treated with recombinant PPI protein exhibited a reduction in the formation of hydrogen peroxide (H2O2)-mediated reactive oxygen species (ROS). In HepG2 cells, treatment of recombinant PPI protein expression diminished H2O2-mediated oxidative stress and restored both the expression and the activity of certain antioxidant enzymes, including superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx) and thioredoxin reductase (TRR). CAT, SOD and TRR activities were upregulated by treatment with the purified protein. CAT mRNA expression was significantly increased in HepG2 cells treated with recombinant PPI protein. These enzymes are the first line of antioxidant defense against ROS generated in times of oxidative stress. Accordingly, data from the present study indicate that the recombinant PPI protein is able to regulate the expression of antioxidant enzymes. Recombinant PPI has antioxidant properties that prevent oxidative stress-induced toxicity, enhance cell viability, decrease ROS production and inhibit oxidative damage and mitochondrial dysfunction in HepG2 cells. Therefore, the present study hypothesizes that the recombinant PPI protein has the potential to protect the liver against oxidative stress-induced cell damage and should be considered as an antioxidant.

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“…The calibration solution was injected at the beginning of the run, and all the spectra were calibrated prior to the identification. The optimum values of the source and transfer parameters were established according to previous research in our laboratory (Abu-Reidah et al, 2012). The acquisition in automated MS/MS mode was of one precursor ion.…”

Section: Analytical Characterizationmentioning

confidence: 99%

RP-HPLC–ESI–QTOF/MS2 based strategy for the comprehensive metabolite profiling of Sclerocarya birrea (marula) bark

Jiménez‐Sánchez

Lozano‐Sánchez

Gabaldón

et al. 2015

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HPLC–ESI-Q-TOF-MS for a comprehensive characterization of bioactive phenolic compounds in cucumber whole fruit extract

Cited by 118 publications

References 40 publications

Antioxidant Activity of Oxygen Evolving Enhancer Protein 1 Purified from Capsosiphon fulvescens

Antioxidant Activity of Oxygen Evolving Enhancer Protein 1 Purified from Capsosiphon fulvescens

Effects of the cyclophilin-type peptidylprolyl cis-trans isomerase from Pyropia yezoensis against hydrogen peroxide-induced oxidative stress in HepG2 cells

RP-HPLC–ESI–QTOF/MS2 based strategy for the comprehensive metabolite profiling of Sclerocarya birrea (marula) bark

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