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Guaiacol

Guaiacol is a phenol compound found in various plant extracts, known for its distinct smoky, medicinal odor.
It is commonly used in the production of vanillin, an important flavor and fragrance compound.
Guaiacol has been studied for its potential therapeutic applications, including as an antioxidant, anti-inflammatory, and antimicrobial agent.
Researchers are actively investigating Guaiacol's effects on various biological processes and its potential use in pharmaceuticals, personal care products, and other industries.
This MeSH term provides a concise overview of the chemical and biological properties of Guaiacol, helping researchers optimize their studies and discover new applications for this versitile compound.

Most cited protocols related to «Guaiacol»

Fresh plant material (1g) was homogenized in 100 mM Tris-HCl (pH 7.5) in presence of DTT (Dithiothreitol, 5 mM), MgCl2 10 mM, Ethylenediaminetetraacetic acid (EDTA, 1 mM), magnesium acetate 5 mM, Polyvinylpyrolidone (PVP-40 1.5%), phenylmethanesulfonyl fluoride (PMSF 1 mM) and aproptinin 1 μgmL-1. After the filtration, the homogenate was centrifuged at 10,000 rpm for 15 min. The supernatant collected after centrifugation served as enzyme source. For the analysis of APX activity, tissues were separately homogenized with 2 mM AsA. All experiments were performed at 4°C.
Activity of SOD was estimated according to Kono (1978) (link) following the photo reduction of nitroblue tetrazolium (NBT). The absorbance was recorded spectrophotometerically (Beckman 640 D, USA) at 540 nm. SOD unit is the quantity of enzyme that hamper 50% photoreduction of NBT and is expressed as EU mg-1 protein.
The activity of POD was estimated according to the method proposed by Putter and Becker (1974) . The rate of production of oxidized guaiacol was estimated spectrophotometerically (Beckman 640 D, USA) at 436 nm. The activity of POD was expressed as EU mg-1 protein.
Catalase activity was estimated by the method of Aebi (1984) (link). The OD was taken spectrophotometerically (Beckman 640 D, USA) at 240 nm and the activity was expressed as EU mg-1 protein.
For the determination of APX activity, the procedure of Nakano and Asada (1981) was used. The OD was recorded at 265 nm by spectrophotometer (Beckman 640 D, USA) and the activity was expressed as EU mg-l protein.
Publication 2016
Catalase Centrifugation Dithiothreitol Edetic Acid Enzymes Filtration Guaiacol magnesium acetate Magnesium Chloride Nitroblue Tetrazolium Phenylmethylsulfonyl Fluoride Plants Proteins PVP 40 Tissues Tromethamine
The SOD (EC 1.15.1.1), CAT (EC 1.11.1.6), GR (EC 1.6.4.2), GPX (EC 1.11.1.9) activities in the samples were determined using Total SOD Assay Kit with WST-1 (S0102, Beyotime, China), CAT Assay Kit (S0051, Beyotime, China), GR Assay Kit (S0055, Beyotime, China) and Total GPX Assay Kit (S0058, Beyotime, China), respectively, according to the manufacturer's instructions. The POD (EC 1.11.1.7) activity was measured with Plant POD Assay Kit (A084-3, Nanjing Jiancheng Bioengineering Institute, China) as the instruction described.
For the determination of SOD activity, 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-(2, 4-disulfophenyl)-2H-tetrazolium (WST-1) method was used [33] (link). WST-1 can couple with xanthine oxidase (XO) to generate O2 and formazan dye, however, this reaction can be inhibited by SOD by catalysing O2 into H2O2 and O2. Therefore, the SOD activity can be calculated by measuring the absorbance of formazan dye at 450 nm.
The CAT activity was assayed using CAT Assay Kit (S0051, Beyotime, China) as previous described [34] . Briefly, the protein supernatants were treated with excess H2O2 for decomposition by CAT for 5 min, and the remaining H2O2 coupled with a substrate was treated with POD to generate a red product, N-4-antipyryl-3-chloro-5-sulfonate-p-benzoquinonemonoimine, which can be examined at 520 nm. CAT activity can be determined by measuring the decomposition of H2O2.
For the GR activity assay, GR Assay Kit (S0055, Beyotime, China) was used. The reaction mixture included 20 µl of sample, 100 µl of GSSG solution, 70 µl of GR assay solution and 10 µl of 2 mM NADPH, and the blank was set without sample. Glutathione disulfide (GSSG) can be catalyzed to reduced glutathione (GSH) by GR in the present of NADPH. Then the GR activity can be determined by measuring the reduction of NADPH from the absorbance at 340 nm.
The GPX activity was determined using Total GPX Assay Kit (S0058, Beyotime, China) as described by Wang et al. [35] (link). Briefly, the reaction mixture contained 10 µl of sample supernatant, 176 µl GPX assay buffer, 10 µl GPX assay working solution (4.8 mM NADPH, 40.4 mM GSH, and GR solution supplied by the kit), 4 µl of 15 mM cumene hydroperoxide (Cum-OOH), and two controls were set without sample and without Cum-OOH, respectively. The GPX activity was calculated by measuring the reduction of NADPH to NADP+ at 340 nm of absorbance.
The POD activity was assayed with Plant POD Assay Kit (A084-3, Nanjing Jiancheng Bioengineering Institute, China) as the instruction described based on the guaiacol oxidation [36] (link). The POD activity was determined by examining the absorbance of reaction buffer at 420 nm.
The relative activities of the above antioxidant enzymes were quantified as fold change in relative to Yukon under control condition for 7 d.
Publication 2012
4-nitrophenyl Alkanesulfonates Antioxidant Activity Biological Assay Buffers cumene hydroperoxide Enzymes Formazans Glutathione Disulfide Guaiacol NADP Peroxide, Hydrogen Plants Proteins Reduced Glutathione Tetrazolium Salts Xanthine Oxidase
HMVEC-D cells were seeded on 1.0 μm Costar transwell inserts coated with fibronectin. Cells were grown to confluency and treated with SecinH3 for 3 hours or MAPK/NF-κB/transcription/translation inhibitors for 30 minutes followed by treatment with 10ng/ml IL-1β. Alternatively, cells were infected with Ad-GFP or Ad-ARF6Q67L adenovirus for 48 hours. siRNA knockdown was performed as described in supplementary methods and cells were treated with IL-1β 72 hours after the second siRNA transfection. Two hours later, horseradish peroxidase (HRP) was added to the top chamber at a final concentration of 100μg/ml. Medium was removed after 60 minutes from the lower chamber. For time-course transwell assays and transcription/translation inhibitor experiments (Figure 1a,c–d), HRP was added to the insert at the same time as IL-1β. Transwell inserts were moved to fresh wells after each timepoint, and the concentration of HRP in the bottom chamber was measured for monolayer permeability. HRP was assessed using media samples obtained from the lower chamber incubated with 0.5 mM of guaiacol and 0.6 mM H2O2. Spectrophotometric analysis of absorbance at 490 nm provided a quantitative evaluation of the amount of HRP that crossed the membrane. Data are presented as mean ± SEM of at least three independent experiments performed in quadruplicate.
A detailed description of all methods is provided in Supplementary Information
Publication 2012
AD 48 Adenovirus Vaccine Biological Assay Cells Fibronectins Guaiacol Horseradish Peroxidase I-kappa B Proteins Interleukin-1 beta Permeability Peroxide, Hydrogen Protein Synthesis Inhibitors RNA, Small Interfering SecinH3 Somatostatin-Secreting Cells Spectrophotometry Tissue, Membrane Transcription, Genetic Transfection
HMVEC-D cells were seeded on 1.0 μm Costar transwell inserts coated with fibronectin. Cells were grown to confluency and treated with SecinH3 for 3 hours or MAPK/NF-κB/transcription/translation inhibitors for 30 minutes followed by treatment with 10ng/ml IL-1β. Alternatively, cells were infected with Ad-GFP or Ad-ARF6Q67L adenovirus for 48 hours. siRNA knockdown was performed as described in supplementary methods and cells were treated with IL-1β 72 hours after the second siRNA transfection. Two hours later, horseradish peroxidase (HRP) was added to the top chamber at a final concentration of 100μg/ml. Medium was removed after 60 minutes from the lower chamber. For time-course transwell assays and transcription/translation inhibitor experiments (Figure 1a,c–d), HRP was added to the insert at the same time as IL-1β. Transwell inserts were moved to fresh wells after each timepoint, and the concentration of HRP in the bottom chamber was measured for monolayer permeability. HRP was assessed using media samples obtained from the lower chamber incubated with 0.5 mM of guaiacol and 0.6 mM H2O2. Spectrophotometric analysis of absorbance at 490 nm provided a quantitative evaluation of the amount of HRP that crossed the membrane. Data are presented as mean ± SEM of at least three independent experiments performed in quadruplicate.
A detailed description of all methods is provided in Supplementary Information
Publication 2012
AD 48 Adenovirus Vaccine Biological Assay Cells Fibronectins Guaiacol Horseradish Peroxidase I-kappa B Proteins Interleukin-1 beta Permeability Peroxide, Hydrogen Protein Synthesis Inhibitors RNA, Small Interfering SecinH3 Somatostatin-Secreting Cells Spectrophotometry Tissue, Membrane Transcription, Genetic Transfection
For extraction of peroxidase (POD, EC 1.11.1.7), catalase (CAT, EC 1.11.1.6) and superoxide dismutase (SOD, EC 1.15.1.1), about 0.5 g of leaf sample was ground in liquid nitrogen with pre-cooled pestle and mortar, and homogenized in 5 ml of extraction buffer containing 50 mM phosphate buffer (pH7.8) and 1% polyvinylpyrrolidone. The homogenate was centrifuged at 10000 g for 20 min at 4°C and the resulting supernatant was collected for enzyme activity analysis. Activities of SOD, expressed as unit (U) ml-1, were spectrophotometrically measured using SOD Detection Kit (A001, Jiancheng, Nanjing, China) according to the manufacturer's instruction. POD activity, expressed as U mg-1 FW, was assayed according to [39 (link)] with slight modification. The assay mixture in a final volume of 3.0 ml, which contained 1 ml of 0.05 M phosphate buffer (pH 7.0), 1 ml of 0.3% H2O2, 0.95 ml of 0.2% guaiacol and 50 μl of enzyme extract, was incubated for 3 min at 34°C. Activity of POD was determined based on the increase in absorbance read at 470 nm, and one unit of POD activity was defined as the increase of absorbance by 0.01 per min. CAT activity was measured by the depletion of H2O2 at 240 nm [53 (link)]. The sample solution was composed of 0.1% H2O2, 100 mM phosphate buffer (pH 7.0) and 100 μl enzyme extract in a total volume of 3 ml. The CAT activity, expressed as U g-1 FW, was assessed by monitoring the decrease in absorbance at 240 nm as a consequence of H2O2 consumption, and one unit of CAT activity was defined as reduction of the absorbance by 0.01 per min.
Publication 2010
Biological Assay Buffers Catalase enzyme activity Enzymes Guaiacol Nitrogen Peroxidase Peroxide, Hydrogen Phosphates Plant Leaves Povidone Superoxide Dismutase

Most recents protocols related to «Guaiacol»

For each treatment, 30 healthy and mature leaves were selected, washed, and dried. Following a 30-min incubation at 105 °C, the leaves were dried at 75 °C, crushed, and screened. The ground leaves were collected in a self-sealing bag and stored in a dryer. Leaf samples were boiled in H2SO4–HClO4 and HNO3–HClO4 solutions and then the nutrient element contents were determined using AutoAnalyzer 3 with XY-2 Sampler (SEAL Analytical, UK) and an inductively coupled plasma emission spectrometer (Prodigy Spec, Teledyne, USA).
On August 10, 10 randomly selected leaves (per treatment) were obtained from OY saplings to measure the catalase (CAT), peroxidase (POD), and superoxide dismutase (SOD) contents as previously described (Wang et al., 2018 (link)). CAT was determined by monitoring the decomposition of H2O2. SOD was assayed by monitoring the inhibition of the photochemical reduction of nitro blue tetrazolium. POD was determined by monitoring the oxidation reaction of guaiacol.
Publication 2023
Catalase Guaiacol Nitroblue Tetrazolium Nutrients Peroxidase Peroxide, Hydrogen Phocidae Plasma Prodigy Psychological Inhibition Superoxide Dismutase
Frozen leaf tissues (200 mg) were obtained through extraction buffer solution consisting of 100 mM phosphate buffer (pH 7.0), 1% polyvinylpyrrolidone 40 (PVP40) (Sigma-Aldrich GmbH, Germany) (w/v), and 0.1 mM disodium ethylenediaminetetraacetate dihydrate (Na2-EDTA) (Sigma-Aldrich GmbH, Germany) to measure the antioxidant enzyme’s activity. Centrifugation of samples was done at 13,000×g for 25 min at 4°C. The supernatant was utilized for further analysis. Bradford (1976) (link) method was used to measure protein content. SOD activity was determined by monitoring the reduction of nitro blue tetrazolium chloride (NBT) (Sigma-Aldrich GmbH, Germany) induced by superoxide radical at 560 nm (Beauchamp and Fridovich, 1971 (link)). One unit of SOD activity was defined as the quantity of enzyme that causes a 50% inhibition of the photochemical reduction of NBT. The measurement of guaiacol peroxidase (POX EC. 1.11.1. 7) activity was performed at 470 nm by utilizing hydrogen peroxide (H2O2) (Sigma-Aldrich GmbH, Germany) and guaiacol (Sigma-Aldrich GmbH, Germany) as substrates. The decline of H2O2 was monitored at 240 nm for the determination of CAT activity (Aebi, 1984 (link)). For the determination of proline content, the ninhydrin method was applied (Bates et al., 1973 (link)).
Publication 2023
2,2'-di-p-nitrophenyl-5,5'-diphenyl-3,3'-(3,3'-dimethoxy-4,4'-diphenylene)ditetrazolium chloride Antioxidant Activity Antioxidants Buffers Centrifugation Edetic Acid enzyme activity Enzymes Freezing Guaiacol guaiacol peroxidase Ninhydrin Peroxide, Hydrogen Phosphates Plant Leaves Povidone Proline Proteins Psychological Inhibition Superoxides Tissues
First, 0.0875 g of
lignin was suspended in DI water with the Ni–Fe cocatalysts
on magnesium silicate supports in a batch reactor. To study the effect
of temperature on the depolymerization of kraft lignin, the system
was studied at temperatures of 250, 300, and 350 °C. Catalysts
were further loaded at 0.0044 g into the reactor. Subsequently, the
reactor was sealed and purged with N2 to remove any reactive
air and achieve an inert atmosphere until reaching 10 bars of N2. The reactor was operated for 1 h with vertical shaking at
40 rpm.
After completing the reaction, the products were separated
by a centrifuge consisting of solid and liquid phases. The solid phase
was defined as char, while the liquid phase contained lignin-derived
products and residual lignin. Next, the liquid phase was acidified
to a pH of 2.00 with 1 M hydrochloric acid. In this step, the residual
lignin was precipitated out as solids by a centrifuge at 15 °C.
Next, the lignin-derived products were separated using ethyl acetate.
Finally, the samples were characterized and quantified by a gas chromatography
mass spectrometer.
The liquid fraction qualification was analyzed
on a GC–MS
instrument (Shimadzu) equipped with a capillary column (30 m ×
0.32 mm × 0.25 mm). The GC heating ramp was as follows: the oven
temperature program increased from 40 °C (held for 3 min) to
300 °C at a rate of 5 °C/min under a helium atmosphere.
The main products from the depolymerization of kraft lignin are anisole,
phenol, p-cresol, 4-ethylphenol, creosol, catechol,
guaiacol, mequinol, 4-ethylguaiacol, syringol, 4-hydroxybenzaldehyde,
vanillin, 4′-hydroxyacetophenone, 3,4-dimethoxyenzaldehyde,
and vanillic acid. These products were analyzed using the database
from the National Institute of Standards and Technology (NIST) for
comparison of the molecular weight. The yields of each product and
the kraft lignin conversion were calculated using the following eqs 1 and 2.
Publication 2023
4-ethylguaiacol 4-ethylphenol 4-hydroxyacetophenone 4-hydroxybenzaldehyde anisole ARID1A protein, human Atmosphere Capillaries Catechols creosol ethyl acetate Guaiacol Helium Hydrochloric acid Kraft lignin Lignin Magnesium mequinol para-cresol Phenol Salvelinus Silicates Syringol Vanillic Acid vanillin
Toluene, cyclopentanone, acetic acid, furfural and guaiacol were mixed with a volume ratio of 1 : 1 : 1 : 1 : 1 to represent simulated bio-oil. All these reagents were analytically pure. The catalytic tests were conducted on a fixed bed reactor, as shown in Fig. S1. For each run, 5 g of catalyst was placed on the insulating spacers of the catalyst reaction bed, and the reaction temperature was 400 °C. Model bio-oil (10 mL) was gasified and introduced into the 400 °C preheated reactor using a peristaltic pump at a flow rate of 20 ml h−1 for 30 min with N2 as the carrier. N2 flushing was maintained for another 20 min after the experiment was complete to ensure that all condensable gas was cooled and collected. The liquid was dissolved in chloroform, and the mass of the liquid after removing chloroform was reported as ML. The yield of liquid after upgrading was defined as follows: where ML is the mass of the upgraded liquid and M0 is the mass of the total simulant component before the reaction.
The conversion of each model component was calculated as follows: where Wa and Wb are the mass of each model component after and before the reaction, respectively. For the regeneration study, the spent catalysts were regenerated using a muffle furnace by heating for 3 h at 550 °C, and then the catalytic activity was tested. The parameters of the regeneration catalytic activity experiments were the same as those of the catalytic tests mentioned above.
Publication 2023
A-A-1 antibiotic Acetic Acid Bio-Oil Catalysis Chloroform cyclopentanone enzyme activity Furaldehyde Guaiacol Peristalsis Regeneration Toluene
The catalase and guaiacol peroxidise activities were assayed as per the protocol of Pereira et al. (2002) (link) and guaiacol peroxidase as per the protocol of Ramiro et al. (2006) (link). CAT activity was measured by following the decomposition of H2O2 at 240 nm in a reaction mixture containing 50 mM phosphate buffer (pH 7.0) and 15 Mm H2O2. Enzyme activity was expressed as Ug-1FW For GPX, the oxidation of guaiacol was measured by following the increase in absorbance at 470 nm for 1 min. The assay mixture contained 50 mM phosphate buffer (pH 7.0), 0.1 mM EDTA, 10 mM guaiacol and 10 mM H2O2. GPOX activity was expressed as µmolg-1min-1
Publication 2023
Biological Assay Buffers Catalase Edetic Acid enzyme activity Guaiacol guaiacol peroxidase Peroxide, Hydrogen Phosphates

Top products related to «Guaiacol»

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Guaiacol is a chemical compound used as a laboratory reagent. It is a colorless to pale yellow liquid with a characteristic smoky, vanilla-like odor. Guaiacol is commonly used as a precursor in the synthesis of various organic compounds.
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Catechol is a chemical compound used in various laboratory applications. It serves as a reagent for the detection and analysis of certain substances. Catechol is commonly employed in analytical chemistry, biochemistry, and related scientific disciplines.
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Vanillin is a chemical compound used as a flavoring agent. It is the primary component of the extract of the vanilla bean and is commonly used in the food, beverage, and pharmaceutical industries.
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Gallic acid is a naturally occurring organic compound that can be used as a laboratory reagent. It is a white to light tan crystalline solid with the chemical formula C6H2(OH)3COOH. Gallic acid is commonly used in various analytical and research applications.
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Hydrogen peroxide is a clear, colorless liquid chemical compound with the formula H2O2. It is a common laboratory reagent used for its oxidizing properties.
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Methanol is a clear, colorless, and flammable liquid that is widely used in various industrial and laboratory applications. It serves as a solvent, fuel, and chemical intermediate. Methanol has a simple chemical formula of CH3OH and a boiling point of 64.7°C. It is a versatile compound that is widely used in the production of other chemicals, as well as in the fuel industry.
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Acetic acid is a colorless, vinegar-like liquid chemical compound. It is a commonly used laboratory reagent with the molecular formula CH3COOH. Acetic acid serves as a solvent, a pH adjuster, and a reactant in various chemical processes.
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ABTS is a laboratory reagent used for the detection and quantification of peroxidase activity. It is a colorimetric substrate that undergoes a color change when oxidized by peroxidases, allowing for spectrophotometric or colorimetric analysis.
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Syringaldehyde is a chemical compound used in various laboratory applications. It serves as a building block for the synthesis of other compounds and as a reagent in analytical procedures. Syringaldehyde is a crystalline solid with a specific molecular structure and chemical properties.
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Ferulic acid is a phenolic compound that can be found in various plant sources, including rice, wheat, oats, and vegetables. It is commonly used as a lab equipment product for research and analysis purposes. Ferulic acid has antioxidant properties and can be used in a variety of applications, such as the study of plant-based compounds and their potential health benefits.

More about "Guaiacol"

Guaiacol, a phenolic compound found in various plant extracts, is known for its distinct smoky, medicinal odor.
This versatile chemical has gained attention for its potential therapeutic applications, including its antioxidant, anti-inflammatory, and antimicrobial properties.
Guaiacol is commonly used in the production of vanillin, an important flavor and fragrance compound, and researchers are actively investigating its effects on biological processes.
Guaiacol is chemically related to other important compounds, such as catechol, which is a precursor to guaiacol, and gallic acid, which shares structural similarities.
Hydrogen peroxide and methanol are also relevant, as they can be used in the synthesis or modification of guaiacol.
Acetic acid and ABTS (2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)) are commonly used in the evaluation of guaiacol's antioxidant activity.
Additionally, syringaldehyde and ferulic acid are other phenolic compounds that may share some functional properties with guaiacol.
By understanding the chemical and biological properties of guaiacol, as well as its relationship to related compounds, researchers can optimize their studies and discover new applications for this versatile substance in pharmaceuticals, personal care products, and other industries.
PubCompare.ai, an innovative tool, can help researchers locate the best reproducible protocols from literature, preprints, and patents, and leverage AI-driven analysis to identify the most effective products for their guaiacol-related research.