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> Phenomena > Natural Phenomenon or Process > Decarboxylation

Decarboxylation

Decarboxylation is the chemical process of removing a carboxyl group (COOH) from a molecule, typically resulting in the release of carbon dioxide (CO2).
This reaction is of great importance in organic chemistry, biochemistry, and various industrial processes.
Decarboxylation plays a crucial role in the metabolism of many biomolecules, such as amino acids, fatty acids, and aromatic compounds.
It is also a key step in the production of various pharmaceuticals, biofuels, and other valuable chemicals.
Researchers studying decarboxylation often utilize optimized protocols and AI-driven comparisons to enhance reproducibility and accuracy in their studies, as offered by tools like PubCompare.ai.
This concise overview provides a general understanding of the decarboxylation process and its significance across multiple fields of science and technology.

Most cited protocols related to «Decarboxylation»

1
Analyzing Cannabis Flower Prices in Washington
Expenditures were measured in US dollars, inclusive of excise taxes but not state or local sales taxes. Trends in product variety were measured using monthly share of expenditures by product type or potency category.
The traceability system reports potency as measured via laboratory testing. THC concentration was calculated as the estimated total weight of THC after decarboxylation as a percent of total item weight (see Supplementary Appendix for details). Similarly, CBD concentration was measured as total weight of CBD as a percent of item weight.
It is worth noting that the integrity of Washington’s accredited cannabis testing laboratories has been challenged. There are anomalies in the data, incentives to produce results favorable to customers, and limited enforcement mechanisms. However, criticism has largely focused on testing for contaminants, not potency [34 ], and on edible products (which we exclude), for which testing is technically more difficult [35 ]. Further, in April 2016, LCB increased enforcement by issuing new rules for a proficiency testing program to hold labs accountable (effective August 2016) [36 ], and in May issued its first laboratory certification suspension [37 ]. Sensitivity analyses motivated by these concerns are provided in the Supplementary Appendix.
For the cannabis flower price analysis, the outcome measure is the item-level excise-tax-inclusive price per gram, calculated as the excise-tax-inclusive price divided by the quantity purchased in grams and log-transformed. Key predictors are item weight (measured in grams and log transformed), as well as the measures of THC and CBD concentration described above.
Additional covariates in the hedonic price regressions were constructed from the reported date of sale. These included separate indicator variables for whether a sale occurred a) within the first three months of a store’s operation to account for store opening discounts, b) on April 20th, widely recognized as a cannabis holiday, c) on the week prior to the cannabis holiday (April 14th to 19th), and d) after June 30, 2015 to account for the change in Washington’s cannabis excise tax. All regressions also controlled for time effects through indicator variables for month, day of month, and day of week, as well as a 5th order polynomial time trend.
Smart R., Caulkins J.P., Kilmer B., Davenport S, & Midgette G. (2017). VARIATION IN CANNABIS POTENCY & PRICES IN A NEWLY-LEGAL MARKET: Evidence from 30 million cannabis sales in Washington State. Addiction (Abingdon, England), 112(12), 2167-2177.
Publication 2017
Cannabis Decarboxylation Hypersensitivity Inclusion Bodies
2
Enzymatic Assays for Cholinergic and Dopaminergic Activities
Cells were harvested as described above and were disrupted by homogenization in a ground-glass homogenizer fitted with a ground-glass pestle, using a buffer consisting of 154 mM NaCl and 10 mM sodium-potassium phosphate (pH 7.4). Aliquots were withdrawn for measurement of DNA and protein (Smith et al. 1985 (link)).
ChAT assays (Lau et al. 1988 (link)) were conducted in 60 μL of a buffer consisting of 60 mM sodium phosphate (pH 7.9), 200 mM NaCl, 20 mM choline chloride, 17 mM MgCl2, 1 mM EDTA, 0.2% Triton X-100, 0.12 mM physostigmine, and 0.6 mg/mL bovine serum albumin (Sigma Chemical Co.), containing a final concentration of 50 μM [14C]acetyl-coenzyme A (specific activity 60 mCi/mmol, diluted with unlabeled compound to 6.7 mCi/mmol; PerkinElmer Life Sciences, Boston, MA). The amount of protein used in each assay was adjusted to maintain activity within the linear range. Blanks contained homogenization buffer instead of the tissue homogenate. Samples were pre-incubated for 15 min on ice and transferred to a 37°C water bath for 30 min; the reaction was terminated by placing the samples on ice. Labeled acetylcholine was then extracted and counted in a liquid scintillation counter and the activity was calculated as nanomoles synthesized per hour per microgram DNA.
TH activity was measured using [14C]tyrosine as a substrate and trapping the evolved 14CO2 after coupled decarboxylation with dopa decarboxylase (Lau et al. 1988 (link); Waymire et al. 1971 (link)). Homogenates were sedimented at 26,000 × g for 10 min to remove storage vesicles containing catecholamines, which interfere with TH activity, and assays were conducted with 100 μL aliquots of the supernatant solution in a total volume of 550 μL. Each assay (pH 6.1) contained final concentrations of 910 μM FeSO4, 55 μM unlabeled L-tyrosine (Sigma Chemical Co.), 9.1 μM pyridoxal phosphate (Sigma Chemical Co.), 36 μM β-mercaptoethanol, and 180 μM 2-amino-6,7-dimethyl-4-hydroxy-5,6,7,8-tetrahydropteridine HCl (Sigma Chemical Co.), all in a buffer of 180 mM sodium acetate and 1.8 mM sodium phosphate (pH 6.1). Each assay contained 0.5 μCi of generally labeled [14C]tyrosine (specific activity, 438 mCi/mmol; Sigma Chemical Co.) as substrate, and blanks contained buffer in place of the homogenate. Activity was calculated on the same basis as for ChAT.
Slotkin T.A., MacKillop E.A., Ryde I.T., Tate C.A, & Seidler F.J. (2006). Screening for Developmental Neurotoxicity Using PC12 Cells: Comparisons of Organophosphates with a Carbamate, an Organochlorine, and Divalent Nickel. Environmental Health Perspectives, 115(1), 93-101.
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Publication 2006
2-Mercaptoethanol 5,6,7,8-tetrahydropteridine Acetylcholine Bath Biological Assay Buffers Catecholamines Cells Choline Chloride Coenzyme A, Acetyl Decarboxylation Dopa Decarboxylase Edetic Acid Magnesium Chloride Physostigmine Potassium potassium phosphate Proteins Pyridoxal Phosphate Scintillation Counters Serum Albumin, Bovine Sodium Sodium Acetate Sodium Chloride sodium phosphate Tissues Triton X-100 Tyrosine
3
Enzymatic Assays for Cholinergic and Dopaminergic Activity
Cells were harvested as described above and were disrupted by homogenization in a ground-glass homogenizer fitted with a ground-glass pestle, using a buffer consisting of 154 mM NaCl and 10 mM sodium-potassium phosphate (pH 7.4). An aliquot was withdrawn for measurement of protein (Smith et al. 1985 (link)).
ChAT assays (Lau et al. 1988 (link)) were conducted with 40 μg of sample protein in 60 μL of a buffer consisting of 60 mM sodium phosphate (pH 7.9), 200 mM NaCl, 20 mM choline chloride, 17 mM MgCl2, 1 mM EDTA, 0.2% Triton X-100, 0.12 mM physostigmine (Sigma), and 0.6 mg/mL bovine serum albumin (Sigma), containing a final concentration of 50 μM [14C]acetyl-coenzyme A (specific activity of 44 mCi/mmol, diluted with unlabeled compound to 6.7 mCi/mmol; PerkinElmer Life Sciences, Boston, MA). Blanks contained homogenization buffer instead of the tissue homogenate. Samples were preincubated for 15 min on ice, transferred to a 37°C water bath for 30 min, and the reaction terminated by placing the samples on ice. Labeled acetylcholine was then extracted and counted in a liquid scintillation counter, and the activity was determined relative to DNA or protein.
TH activity was measured using [14C]tyrosine as a substrate and trapping the evolved 14CO2 after coupled decarboxylation with DOPA decarboxylase (Lau et al. 1988 (link); Waymire et al. 1971 (link)). Homogenates were sedimented at 26,000 × g for 10 min to remove storage vesicles containing catecholamines, which interfere with TH activity, and assays were conducted with 100 μL aliquots of the supernatant solution in a total volume of 550 μL. Each assay contained final concentrations of 910 μM FeSO4, 55 μM unlabeled l-tyrosine (Sigma), 9.1 μM pyridoxal phosphate (Sigma), 36 μM β-mercaptoethanol, and 180 μM 2-amino-6,7-dimethyl-4-hydroxy-5,6,7,8-tetrahydropteridine HCl (Sigma), all in a buffer of 180 mM sodium acetate and 1.8 mM sodium phosphate (pH 6.1). Each assay contained 0.5 μCi of generally labeled [14C]tyrosine (specific activity, 438 mCi/mmol; Sigma) as substrate, and blanks contained buffer in place of the homogenate.
Jameson R.R., Seidler F.J., Qiao D, & Slotkin T.A. (2005). Chlorpyrifos Affects Phenotypic Outcomes in a Model of Mammalian Neurodevelopment: Critical Stages Targeting Differentiation in PC12 Cells. Environmental Health Perspectives, 114(5), 667-672.
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Publication 2005
2-Mercaptoethanol 5,6,7,8-tetrahydropteridine Acetylcholine Bath Biological Assay Buffers Catecholamines Cells Choline Chloride Coenzyme A, Acetyl Decarboxylation Dopa Decarboxylase Edetic Acid Magnesium Chloride Physostigmine Potassium potassium phosphate Proteins Pyridoxal Phosphate Scintillation Counters Serum Albumin, Bovine Sodium Sodium Acetate Sodium Chloride sodium phosphate Tissues Triton X-100 Tyrosine
4
Standardized CBD Extract Characterization
CBD extract was prepared following GMP procedures from the leaves and flowering tops by the extraction of CBD rich cannabis plant material (5.61% of CBD and 0.2% THC) using hexane as the extraction solvent. The extract was then evaporated to dryness followed by raising the temperature to 80 °C to effect complete decarboxylation of the extract. The final extract was analyzed using GC/MS for its cannabinoid content, solvent residue, heavy metals, bacterial and fungal counts and aflatoxin content following USP procedures. The results showed the following: cannabidiol content 57.9%; other cannabinoids: cannabichromene 2.03%, Δ9-tetrahydrocannabinol 1.69%, cannabigerol 1.07%, Δ8-tetrahydrocannabinol <0.01%; tetrahydrocannabivarin <0.01%. Residual solvent <0.5%; loss on drying 0.32%; heavy metals: lead, mercury, cadmium, and arsenic were not detected; aflatoxins: AFB1, AFB2, AGF1, AFG2 were not detected.
Doses of the CBD extract were calculated based on the CBD content listed above to deliver the required dose of CBD. For simplicity, the ‘CBD-rich cannabis extract’ will be referred to as ‘CBD’ throughout this manuscript. The extract was diluted in sesame oil to prepare the gavage solution. Allometric scaling for CBD mouse equivalent doses (MED) was determined per the recommendation of Wojcikowski and Gobe which, in turn, is based upon the FDA Industry Guidance for Estimating the Maximum Safe Starting Dose in Initial Clinical Trials for Therapeutics in Adult Volunteers [40 (link)]. The scaling factor of 12.3, commonly used for mice weighing between 11–34 g, was used to calculate the MED for CBD. The MED was based on the maximum recommended human maintenance dose of CBD (Epidiolex®), which is 20 mg/kg. For the 1× dose, the quantity of CBD administered was 20 mg/kg × 0.025 kg (average mouse weight in our study) × 12.3 (scaling factor for mice) = 6.15 mg total CBD delivered in 300 µL of gavage solution or 246 mg/kg. Consequently, 3× dose = 18.45 mg total CBD in 300 µL gavage solution or 738 mg/kg), and 10× dose = 61.5 mg total CBD in 300 µL gavage solution or 2460 mg/kg). In the sub-acute study, the dose of 61.5 mg/kg (MED of 5 mg/kg CBD) was considered as 1× dose. Consequently, the doses of 184.5 mg/kg (MED of 15 mg/kg CBD) and 615 mg/kg (MED of 50 mg/kg CBD) were considered as 3× and 10×, respectively. Control mice received 300 µL of sesame oil.
Ewing L.E., Skinner C.M., Quick C.M., Kennon-McGill S., McGill M.R., Walker L.A., ElSohly M.A., Gurley B.J, & Koturbash I. (2019). Hepatotoxicity of a Cannabidiol-Rich Cannabis Extract in the Mouse Model. Molecules, 24(9), 1694.
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Publication 2019
Adult Aflatoxins Arsenic Bacteria Cadmium cannabichromene cannabigerol Cannabinoids Cannabis Cannabis sativa Decarboxylation Dronabinol Epidiolex Factor XII Flowering Tops Fungal Count Gas Chromatography-Mass Spectrometry Hexanes Homo sapiens Mercury Metals, Heavy Mice, House Sesame Oil Solvents Therapeutics Tube Feeding Voluntary Workers
5
Screening Non-Conventional Yeasts for Biogenic Amines
To confirm that the non-conventional yeast strains shortlisted here (Table 1) are safe to use, we checked that none produced any biogenic amines (BAs). Production of BAs was determined using an adapted version of the method explained by Joosten and Northholt [28 (link), 29 (link)]. Briefly, yeast strains (106 cells per ml) were inoculated onto YPD agar plates supplemented with bromocresol purple (Sigma Aldrich) 0.006% and an amino acid mix with a total mass concentration of 1% (MP Biochemicals, LLC). The added amino acids are tyrosine, histidine, phenylalanine, leucine, tryptophan, arginine and lysine at equal ratios. Subsequently, the plates were incubated at 30°C for 7 days and the growth and changes in the color of the medium was monitored daily to test for the presence of BAs. In strains with no BA production, the growth area was surrounded by a yellow halo caused by glucose fermentation, followed by a pH reduction that causes the medium to turn purple after a period that depends on the growth rate of the strain. By contrast, when BAs are produced, amino acid decarboxylation resulted in a purple halo from the very beginning, which grew bigger and darker as a function of time.
Aslankoohi E., Herrera-Malaver B., Rezaei M.N., Steensels J., Courtin C.M, & Verstrepen K.J. (2016). Non-Conventional Yeast Strains Increase the Aroma Complexity of Bread. PLoS ONE, 11(10), e0165126.
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Publication 2016
Agar Amino Acids Arginine Biogenic Amines Bromcresol Purple Cells Darkness Decarboxylation Fermentation Glucose Histidine Leucine Lysine Phenylalanine Strains Tryptophan Tyrosine Yeast, Dried

Most recents protocols related to «Decarboxylation»

1
Salmonella Serotyping and Identification
All isolates were serotyped by slide agglutination of O and H antigens according to the instructions provided by the manufacturer of the antiserum that we used (Ningbo Tianrun Bio-technology Co., LTD., China). The serotypes could then be determined according to the Kauffmann–White classification scheme [39 ]. For the identification of S. gallinarum and S. pullorum, dulcitol fermentation and ornithine decarboxylation tests were conducted according to a previous study [40 (link)]. Salmonella biochemical identification tubes were purchased from Hangzhou Microbial Reagent Co., Ltd. (Hangzhou, China). PCR was performed on isolates identified as S. pullorum using a specific IpaJ gene for S. pullorum (Table S1); the standard strain of S. pullorum (CVCC 526) purchased from the China Center for the Preservation and Management of Veterinary Microorganisms was used as a positive control and S. enteritidis (CVCC 3377) was used as a negative control.
Shi W., Tang W., Li Y., Han Y., Cui L, & Sun S. (2023). Comparative Analysis between Salmonella enterica Isolated from Imported and Chinese Native Chicken Breeds. Microorganisms, 11(2), 390.
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Publication 2023
Agglutination Biologic Preservation Decarboxylation Dulcitol Fermentation Genes, vif H antigen, bacterial Immune Sera Ornithine Salmonella Salmonella enteritidis Strains
2
Consensus Metabolic Model of E. coli
The “consensus” E. coli core metabolic model [41 (link)] was used with minor changes (see Supplementary Materials Table S1). Briefly, the model included the main pathways of E. coli glucose metabolism: Embden−Meyerhof−Parnas (EMP), pentose−phosphate (PP), and Entner−Doudoroff (ED), the tricarboxylic acid (TCA) cycle, the glyoxylate shunt, anaplerotic carboxylation, and decarboxylation of malate and oxaloacetate. For the transketolase (EC 2.2.1.1, TK) and transaldolase (EC 2.2.1.2, TA) reactions, a ping-pong mechanism of their action was considered, and reactions were modeled as metabolite specific, reversible, C2 and C3 fragment producing, and consuming half-reactions of TK-C2 and TA-C3 [42 (link)].
The fructose-1,6-bisphosphatase and phosphoenolpyruvate synthetase reactions were added to the model, as cells grown on glucose minimal medium possess these enzymes [43 (link),44 (link),45 (link)]. The energy-consuming futile cycles composed of reactions catalyzed by these two enzymes and by corresponding partners, such as 6-phosphofructokinase or pyruvate kinase reactions [46 (link),47 (link),48 (link),49 (link)], can affect the central metabolism of the cells [50 (link)]. Two alternative pathways for acetate synthesis were considered: first, acetate synthesis from acetyl-CoA via reversible reactions of the phosphate acetyltransferase and acetate kinase and, second, acetate synthesis from pyruvate via an irreversible pyruvate oxidase reaction. Both pathways are known to be active in E. coli [51 (link),52 (link),53 (link)]. Accounting for both pathways for acetate synthesis may affect the accuracy of the pyruvate dehydrogenase (PDH) flux estimation. Thus, the PDH flux was characterized by an interval in which the lower boundary was limited by the acetyl-CoA requirement for biomass synthesis and the upper boundary was determined under the assumption that all secreted acetate is synthesized from acetyl-CoA.
To account for CO2-associated carbon transfer, reactions accompanied by CO2 production or consumption were expressed in an explicit manner including an anabolic reaction and a reaction of CO2 exchange with an environment modeled as specified in [54 (link)].
Two known pathways for the glycine synthesis in E. coli, from serine and threonine [55 (link)], were included into the model. According to the previously performed analysis of cells grown aerobically on 13C-labeled glucose, the glycine cleavage is irreversible [56 (link)].
The reversible reactions were modeled as described in [57 (link)], that is, as forward (F) and reverse (R) fluxes, the difference between which gives a value of net flux through the reversible reaction.
The amino acid biosynthesis reactions, data on the mass isotopomer distribution (MID) of which were used for flux calculation, were explicitly expressed. To account for carbon transfer associated with biomass synthesis, reactions of nucleotides biosynthesis were explicitly expressed as well. One example is carbon transfer from the aspartate pool to the fumarate pool when aspartate is used as a donor of the amino group. Metabolites drained for biomass synthesis were accounted for by a single biomass equation, as described in Section 2.9.4.
Atom transition schemes were extracted from the literature [58 (link)]. The measured external carbon fluxes (effluxes) were biomass synthesis, efflux of secreted acetate, and the glucose uptake rate.
Malykh E.A., Golubeva L.I., Kovaleva E.S., Shupletsov M.S., Rodina E.V., Mashko S.V, & Stoynova N.V. (2023). H+-Translocating Membrane-Bound Pyrophosphatase from Rhodospirillum rubrum Fuels Escherichia coli Cells via an Alternative Pathway for Energy Generation. Microorganisms, 11(2), 294.
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Publication 2023
6-Phosphofructokinase Acetate Acetate Kinase Amino Acids Anabolism Androgens, Synthetic Aspartate Biosynthetic Pathways Carbon Carbon Cycle Cells Citric Acid Cycle Coenzyme A, Acetyl Cytokinesis Decarboxylation Drug Kinetics Enzymes Escherichia coli Fructose Fumarate Futile Cycles Glucose Glycine glyoxylate Ligase malate Metabolism Nucleotides Oxaloacetate Oxidoreductase Pentosephosphates Phosphate Acetyltransferase Phosphoenolpyruvate Pyruvate Pyruvate Kinase Pyruvate Oxidase Serine Threonine Tissue Donors Transaldolase Transketolase
3
Radiolabeling Bacterial Cell Wall Components
Unless otherwise stated, radiolabeling was performed in the Escherichia coli FB8-LysA strain which is unable to convert meso-diaminopimelic acid (mesoDAP) to lysine by decarboxylation (55 (link)). Therefore, mesoDAP added to the growth media is incorporated specifically into the peptidoglycan layer. E. coli FB8-LysA was cultured on LB Miller agar (BD Difco) containing 25 mg/mL kanamycin (Merck). Several colonies were inoculated into 50 mL LB medium plus 25 mg/mL kanamycin and incubated at 37 °C. At approximately OD600 1.0, the preculture was used to inoculate (1:100) 1L prewarmed M9 minimal media supplemented with 100 µg/mL threonine, methionine, and lysine (Merck). For 3H-mesoDAP labeling, 50 µCi/L 3H-meso diaminopimelic acid (3H-mesoDAP; Moraveck Inc.) was added. For 14C-GlcNAc labeling of Escherichia coli, culture was performed in M9 media using 100 μM GlcNAc (Merck) as the carbon source, and spiked with 10 μCi/L 14C-N-acetylglucosamine (14C-GlcNAc; ARC). Cultures were incubated overnight at 37 °C with aeration. Final OD600 was approximately 2.0. Bacteria were harvested by centrifugation at 4,000 × g, resuspension in a small volume of cold H2O, and dropped into 20 mL of 4% SDS in a boiling bain-marie. After 1 h boiling with vigorous agitation, the suspension was cooled to room temperature, and centrifugated at 13,000 × g. The supernatant was discarded, and the pellet resuspended with 20 mL H2O. The radiolabeled cell wall material was washed by centrifugation and resuspension of the pellet with H2O, until the presence of SDS in the supernatant could no longer be detected using the method of Hayashi (56 (link)). The pellet was then resuspended in 4 mL of 50 mM Tris pH 7.5 (Merck), and incubated at 37 °C with 100 µg/mL alpha-amylase (Merck) for 2 h, followed by 2 h incubation with RNase, DNase, and MgCl2, then incubated overnight with 100 µg/mL 3× crystallized trypsin (Worthing Biochemical Corporation) and CaCl2. The pellet was incubated for 15 min at 100 °C, then washed once with H20. Radiolabeled peptidoglycan was stored at −20 °C. For gavage of mice, peptidoglycan was digested overnight with 100 U/mg mutanolysin (from Streptomyces globisporus ATCC 21553, Merck) in 12.5 mM sodium phosphate pH 5.6 (Merck) at 37 °C. Radiolabeling of L. rhamnosus Lr32 was described previously (10 (link)).
Wheeler R., Bastos P.A., Disson O., Rifflet A., Gabanyi I., Spielbauer J., Bérard M., Lecuit M, & Boneca I.G. (2023). Microbiota-induced active translocation of peptidoglycan across the intestinal barrier dictates its within-host dissemination. Proceedings of the National Academy of Sciences of the United States of America, 120(4), e2209936120.
Publication 2023
Acetylglucosamine Agar alpha-Amylases Bacteria Carbon Cell Wall Centrifugation Cold Temperature Decarboxylation Deoxyribonucleases Diaminopimelic Acid Escherichia coli Kanamycin Lysine Magnesium Chloride Methionine Mus mutanolysin Peptidoglycan Ribonucleases sodium phosphate Strains Streptomyces globisporus Threonine Tromethamine Trypsin Tube Feeding
4
Comprehensive Cannabinoid Analysis by HPLC-NMR
HPLC-PDA-ELSD-ESIMS data were recorded on an 8030 triple quadrupole ESIMS system connected to an HPLC system consisting of a degasser, binary high-pressure mixing pump, autosampler, column oven, and photodiode array detector (all Shimadzu). An Alltech 3300 ELSD detector was connected between the photodiode array and the MS detector via a T splitter. HPLC separations were carried out on a Waters SunFireTM C18 column (3.5 μm, 3.0 × 150 mm i.d.) equipped with a guard column (3 × 10 mm i.d). Mobile phase: water + 0.1% formic acid (A), acetonitrile + 0.1% formic acid (B); 70% B (0–2 min), 70–77% B (2–20 min), 77–100% B (20–25 min), 100% B (25–29 min). Extracts were diluted 40-fold, and the injection volume was 2 μL. Analytical standards were used for identification and quantification of THC, CBD, and CBG. Serial dilutions with eight concentrations ranging from 7.8 μg/mL to 1 mg/mL were prepared in triplicate.
For NMR analysis, 50 µL of each extract was dried under a flow of N2. The residue was dissolved in 500 µL CDCl3, and spectra were recorded at 23°C on an Avance Ultrashield NMR Spectrometer (Bruker) operating at 500 MHz for 1H. 1H, HSQC-DEPT, and HMBC spectra were recorded using a BBO-probe head. To enable quantitative evaluation of the integrals, 1H spectra were recorded with an extended relaxation delay D1 of 63 s. ACD/Spectrus Processor software (ACD/Labs) was used for data evaluation. Relative quantification of cannabinoids was performed by using the integrals of prominent signals of each compound. For an intuitive comparison, the relative contents of other cannabinoids are then given in percent relative to the main cannabinoid. As the CH2−1″ signal of the pentyl side chain of cannabinoid acids is typically found in the region between δH 2.75 and 2.90 ppm without the interference from other cannabinoids [25 (link), 26 (link)], this region was integrated and compared to the sum of THC, CBD, and CBG identified in the sample. This allowed to estimate the amount of cannabinoid acids left in the extract after decarboxylation.
Treyer A., Reinhardt J.K., Eigenmann D.E., Oufir M, & Hamburger M. (2023). Phytochemical Comparison of Medicinal Cannabis Extracts and Study of Their CYP-Mediated Interactions with Coumarinic Oral Anticoagulants. Medical Cannabis and Cannabinoids, 6(1), 21-31.
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Publication 2023
acetonitrile Acids Cannabinoids Decarboxylation formic acid Head High-Performance Liquid Chromatographies Pressure Technique, Dilution
5
Salmonella and Shigella Identification
By using a sterile wire loop, the stool sample was inoculated into MacConkey agar (Oxoid Ltd) and incubated at 37°C aerobically for 24 h. Then, non-lactose fermenting colorless/pale colonies were inoculated into Xylose Lysine Deoxycholate (XLD) agar (Oxoid Ltd) and Salmonella Shigella (SS) agar (Oxoid Ltd) and incubated aerobically at 37°C for 24 h. Finally, pink to red colonies on XLD agar and colorless colonies on SS agar with or without black centers were further analyzed with biochemical tests for the identification of Salmonella serovars and Shigella species (6 (link)).
Biochemical tests were performed on pink to red colonies from XLD agar and/or colorless colonies from SS agar with or without black centers for the identification of the Salmonella serovars and Shigella species. Bacteria were identified by using triple sugar iron agar (TSI; H2S and gas production, carbohydrate fermentation), motility test, indole test, citrate utilization test, urea hydrolysis test, lysine decarboxylation (LDC), mannitol fermentation, and oxidase tests.
Dessale M., Mengistu G, & Mengist H.M. (2023). Prevalence, antimicrobial resistance pattern, and associated factors of Salmonella and Shigella among under five diarrheic children attending public health facilities in Debre Markos town, Northwest Ethiopia. Frontiers in Public Health, 11, 1114223.
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Publication 2023
Agar Bacteria Carbohydrates Citrates Decarboxylation Deoxycholate Feces Fermentation Hydrolysis indole Iron Lactose Lysine Mannitol Motility, Cell Oxidases Salmonella Shigella Sterility, Reproductive Sugars Urea Xylose

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More about "Decarboxylation"

Decarboxylation is the fundamental chemical process of removing a carboxyl group (COOH) from a molecule, usually resulting in the release of carbon dioxide (CO2).
This essential reaction holds immense significance across diverse fields, including organic chemistry, biochemistry, and various industrial applications.
The decarboxylation process plays a pivotal role in the metabolism of numerous biomolecules, such as amino acids, fatty acids, and aromatic compounds.
It's a crucial step in the production of various pharmaceuticals, biofuels, and other valuable chemicals.
Researchers working on decarboxylation often leverage optimized protocols and AI-driven comparisons to enhance the reproducibility and accuracy of their studies, as offered by tools like PubCompare.ai.
Decarboxylation is closely related to the functions of other analytical instruments, such as the Centro LB 960 Microplate Luminometer, Cary 50 Bio spectrophotometer, and SpectraMax 190, which are widely used in chemical and biochemical analyses.
Additionally, the decarboxylation of compounds like Catechin gallate, Bromocresol purple, EGCG, Sodium gallate, and Octyl gallate has been extensively studied and documented.
Ammonium sulfate, a common chemical used in various purification and precipitation processes, is also relevant to decarboxylation studies, as it can influence the solubility and stability of decarboxylated products.
By understanding the nuances of decarboxylation and leveraging the insights provided by advanced analytical tools and AI-driven comparisons, researchers can unlock new possibilities in their scientific endeavors and drive progress in fields ranging from pharmaceuticals to biofuels.
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