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Cas Database




  • Product Name:Acetic acid

  • CAS Number: 64-19-7

  • EINECS:200-580-7

  • Molecular Weight:60.0526

  • Molecular Formula: C2H4O2

  • HS Code:29152100

  • Mol File:64-19-7.mol

Synonyms:Acetic acid, diluted;Acetic acid, aqueous solution;Ethanoic acid;Ethanoic acid monomer;Ethylic acid;Glacial acetic acid;Methanecarboxylic acid;Vinegar acid;Glacial acetic acid (JP14);Acetic acid;

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Safety information and MSDS view more

  • Pictogram(s):CorrosiveC,IrritantXi

  • Hazard Codes: C:Corrosive;

  • Signal Word:Danger

  • Hazard Statement:H226 Flammable liquid and vapourH314 Causes severe skin burns and eye damage

  • First-aid measures: General adviceConsult a physician. Show this safety data sheet to the doctor in attendance.If inhaled Fresh air, rest. Half-upright position. Refer immediately for medical attention. In case of skin contact Remove contaminated clothes. Rinse and then wash skin with water and soap. Rinse skin with plenty of water or shower for at least 15 minutes. Refer immediately for medical attention. In case of eye contact Rinse with plenty of water (remove contact lenses if easily possible). Refer immediately for medical attention. If swallowed Rinse mouth. Do NOT induce vomiting. If within a few minutes after ingestion, one small glass of water may be given to drink. Refer immediately for medical attention. Breathing of vapors causes coughing, chest pain, and irritation of nose and throat; may cause nausea andvomiting. Contact with skin and eye causes burns. (USCG, 1999)Excerpt from ERG Guide 153 [Substances - Toxic and/or Corrosive (Combustible)]: TOXIC; inhalation, ingestion or skin contact with material may cause severe injury or death. Contact with molten substance may cause severe burns to skin and eyes. Avoid any skin contact. Effects of contact or inhalation may be delayed. Fire may produce irritating, corrosive and/or toxic gases. Runoff from fire control or dilution water may be corrosive and/or toxic and cause pollution. (ERG, 2016)Excerpt from ERG Guide 132 [Flammable Liquids - Corrosive]: May cause toxic effects if inhaled or ingested/swallowed. Contact with substance may cause severe burns to skin and eyes. Fire will produce irritating, corrosive and/or toxic gases. Vapors may cause dizziness or suffocation. Runoff from fire control or dilution water may cause pollution. (ERG, 2016) Garlic contains many sulfhydryl compounds that act as antioxidants. However, the role of nitric oxide (NO) in inflammation is controversial. The aim of the present study is to investigate the possible protective effect of garlic against acetic acid-induced ulcerative colitis in rats, as well as the probable modulatory effect of L-arginine (NO precursor) on garlic activity. Intra-rectal inoculation of rats with 4% acetic acid for 3 consecutive days caused a significant increase in the colon weight and marked decrease in the colon length. In addition, acetic acid induced a significant increase in serum levels of nitrate as well as colonic tissue content of malondialdehyde (MDA). Moreover, colonic tissue contents of glutathione (GSH), superoxide dismutase (SOD) and catalase (CAT) were markedly reduced. On the other hand, pre-treatment of rats with garlic (0.25 g/kgbwt, orally) for 4 consecutive weeks and 3 days during induction of colitis significantly reduced the increase in the colon weight induced by acetic acid and ameliorated alterations in oxidant and antioxidant parameters. Interestingly, oral co-administration of garlic (0.25 g/kgbwt) and L-arginine (625 mg/kgbwt) for the same period of garlic administration mitigated the changes in both colon weight and length induced by acetic acid and increased garlic effect on colon tissue contents of MDA and GSH. In conclusion, L-arginine can augment the protective effect of garlic against ulcerative colitis; an effect that might be mainly attributed to its NO donating property resulting in enhancement of garlic antioxidant effect...

  • Fire-fighting measures: Suitable extinguishing media Use water spray, dry chemical, "alcohol resistant" foam, or carbon dioxide. Use water to keep fire-exposed containers cool. Special Hazards of Combustion Products: Irritating vapor generated when heated. (USCG, 1999)Excerpt from ERG Guide 153 [Substances - Toxic and/or Corrosive (Combustible)]: Combustible material: may burn but does not ignite readily. When heated, vapors may form explosive mixtures with air: indoors, outdoors and sewers explosion hazards. Those substances designated with a (P) may polymerize explosively when heated or involved in a fire. Contact with metals may evolve flammable hydrogen gas. Containers may explode when heated. Runoff may pollute waterways. Substance may be transported in a molten form. (ERG, 2016)Excerpt from ERG Guide 132 [Flammable Liquids - Corrosive]: Flammable/combustible material. May be ignited by heat, sparks or flames. Vapors may form explosive mixtures with air. Vapors may travel to source of ignition and flash back. Most vapors are heavier than air. They will spread along ground and collect in low or confined areas (sewers, basements, tanks). Vapor explosion hazard indoors, outdoors or in sewers. Those substances designated with a (P) may polymerize explosively when heated or involved in a fire. Runoff to sewer may create fire or explosion hazard. Containers may explode when heated. Many liquids are lighter than water. (ERG, 2016) Wear self-contained breathing apparatus for firefighting if necessary.

  • Accidental release measures: Use personal protective equipment. Avoid dust formation. Avoid breathing vapours, mist or gas. Ensure adequate ventilation. Evacuate personnel to safe areas. Avoid breathing dust. For personal protection see section 8. Remove all ignition sources. Personal protection: chemical protection suit including self-contained breathing apparatus. Do NOT let this chemical enter the environment. Collect leaking liquid in sealable containers. Cautiously neutralize spilled liquid with sodium carbonate only under the responsibility of an expert. Collect leaking liquid in sealable containers. Cautiously neutralize spilled liquid with sodium carbonate only under the responsibility of an expert. Wash away remainder with plenty of water (extra personal protection: chemical protection suit including self-contained breathing apparatus).

  • Handling and storage: Avoid contact with skin and eyes. Avoid formation of dust and aerosols. Avoid exposure - obtain special instructions before use.Provide appropriate exhaust ventilation at places where dust is formed. For precautions see section 2.2. Fireproof. Separated from food and feedstuffs, strong oxidants, strong acids and strong bases. Store only in original container. Well closed. Keep in a well-ventilated room. Store in an area without drain or sewer access.Store in a dry, well-ventilated place. Separate from oxidizing materials and alkaline substances.

  • Exposure controls/personal protection:Occupational Exposure limit valuesRecommended Exposure Limit: 10-hour Time-Weighted Average: 10 ppm (25 mg/cu m).Recommended Exposure Limit: 15-minute Short-Term Exposure Limit: 15 ppm (37 mg/cu m).Biological limit values Handle in accordance with good industrial hygiene and safety practice. Wash hands before breaks and at the end of workday. Eye/face protection Safety glasses with side-shields conforming to EN166. Use equipment for eye protection tested and approved under appropriate government standards such as NIOSH (US) or EN 166(EU). Skin protection Wear impervious clothing. The type of protective equipment must be selected according to the concentration and amount of the dangerous substance at the specific workplace. Handle with gloves. Gloves must be inspected prior to use. Use proper glove removal technique(without touching glove's outer surface) to avoid skin contact with this product. Dispose of contaminated gloves after use in accordance with applicable laws and good laboratory practices. Wash and dry hands. The selected protective gloves have to satisfy the specifications of EU Directive 89/686/EEC and the standard EN 374 derived from it. Respiratory protection Wear dust mask when handling large quantities. Thermal hazards

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Relevant articles and documentsAll total 1910 Articles be found



, p. 1853 (1953)



Makarov, A. P.,Gekhman, A. E.,Polotnyuk, O. Ya.,Moiseev, I. I.

, p. 1749 - 1752 (1985)


Peroxy Acid Oxidations. II. A Kinetic and Mechanistic Study of Oxidation of α-Diketones

Panda, Radhasyam,Panigrahi, Akhil Krishna,Patnaik, Chakrapani,Sahu, Sabita Kumari,Mahapatra, Sabita Kumari

, p. 1363 - 1368 (1988)

The kinetics of Baeyer-Villiger oxidation of biacetyl and benzil by peroxomonophosphoric acid and peroxomonosulfuric acid have been studied in different pH ranges at 308 K.The reactions are second order; first order each in peroxy acid and in diketone concentrations at constant pH.The oxidation rate is strongly pH-dependent; the rate increases with increase in pH.From the pH-rate data the reactivity of different peroxo species, in the oxidation, has been determined.A mechanism consistent with rate-detemining nucleophilic attack of peroxo species on carbonyl carbon of the diketone molecule has been proposed.Acetic acid and benzoic acid are respectively found to be the products of oxidation of biacetyl and benzil.

Kinetics of formation of peroxyacetic acid


, p. 1125 - 1130 (2005)

The kinetics of the reaction of acetic acid with hydrogen peroxide, leading to peroxyacetic acid, were studied at various molar reactant ratios (AcOH-H2O2 from 6 : 1 to 1 : 6) at 20, 40, and 60°C and sulfuric acid (catalyst) concentrations of 0 to 9 wt %. The reaction is reversible, and the equilibrium constant decreases as the temperature rises: K = 2.10 (20°C), 1.46 (40°C), 1.07 (60°C); Δr H 0 = - 13.7±0.1 kJ mol-1, Δr S = -40.5±0.4 J mol-1 K-1. The maximal equilibrium concentration of peroxyacetic acid (2.3 M) is attained at 20°C and a molar AcOH-to-H2O2 ratio of 2.5 : 1. The rate constants of both forward and reverse reactions increase with increase in sulfuric acid concentration from 0 to 5 wt %. Further raising the catalyst concentration does not affect the reaction rate. The reaction mechanism is discussed. 2005 Pleiades Publishing, Inc.

A high-throughput pH-based colorimetric assay: application focus on alpha/beta hydrolases

Paye, Mariétou F.,Rose, Harrison B.,Robbins, John M.,Yunda, Diana A.,Cho, Seonggeon,Bommarius, Andreas S.

, p. 80 - 90 (2018)

Research involving α/β hydrolases, including α-amino acid ester hydrolase and cocaine esterase, has been limited by the lack of an online high throughput screening assay. The development of a high throughput screening assay capable of detecting α/β hydrolase activity toward specific substrates and/or chemical reactions (e.g., hydrolysis in lieu of amidase activity and/or synthesis instead of thioesterase activity) is of interest in a broad set of scientific questions and applications. Here we present a general framework for pH-based colorimetric assays, as well as the mathematical considerations necessary to estimate de novo the experimental response required to assign a ‘hit’ or a ‘miss,’ in the absence of experimental standard curves. This combination is valuable for screening the hydrolysis and synthesis activity of α/β hydrolases on a variety of substrates, and produces data comparable to the current standard technique involving High Performance Liquid Chromatography (HPLC). In contrast to HPLC, this assay enables screening experiments to be performed with greater efficiency.

Kinetic studies on the oxidation of iodide by peroxyacetic acid

Awad, Mohamed Ismail,Oritani, Tadato,Ohsaka, Takeo

, p. 253 - 256 (2003)

The kinetics of the oxidation of iodide by peroxyacetic acid (PAA) in aqueous media in the presence and absence of the heptamolybdate has been studied by a high time resolution spectrophotometric stopped-flow method. The time-dependent concentration of the liberated iodine was monitored by the change in absorbance at 352 nm. The effect of ammonium heptamolybdate as well as pH on the rate of the reaction was also studied and it was found that the rate of the reaction is independent of pH and molybdate concentration under the examined conditions. The results obtained show that the rate law of the reaction can be expressed as rate=k[PAA][I-] with a value of k=4.22×102 (mole/l)-1 s-1 at pH 3.5-5.4 and 25°C.

Activity, recyclability, and stability of lipases immobilized on oil-filled spherical silica nanoparticles with different silica shell structures

Kuwahara, Yasutaka,Yamanishi, Takato,Kamegawa, Takashi,Mori, Kohsuke,Yamashita, Hiromi

, p. 2527 - 2536 (2013)

Candida antarctica lipaseA was immobilized on spherical silica nanoparticles with oil-filled core and oil-induced mesoporous silica shell with different silica shell structures. The immobilization of enzymes was achieved by directly adding enzymes to the oil-in-water emulsion system under ambient synthesis conditions, and the silica shell structure was controlled by the addition of the cosolvent ethanol to the initial synthesis medium. Detailed structural analysis revealed the formation of oil-filled spherical silica nanoparticles with 3.4-4.2nm mesopores randomly arranged in the silica shell; the thickness and pore characteristics of these pores markedly changed with the addition of ethanol. The retention of the enzyme activity during biocatalysis was significantly affected by the structural properties of the silica shells, and it was found that a thick and dense silica shell is essential to afford an active, recyclable, and stable biocatalyst. Furthermore, the oil encapsulated within the core cavity was found to play an important role in achieving a high catalytic efficiency. Trapped oil: Candida antarctica lipaseA is immobilized on oil-filled spherical silica nanoparticles with different silica shell structures through an anionic surfactant-induced self-assembly approach (see scheme) with ethanol as a cosolvent. The entrapped enzymes mostly retain their activities and exhibit recyclability and thermal and chemical stability, depending on the thickness and pore characteristics of the silica shells. TEOS=Tetraethoxyorthosilicate, APTES=3-aminopropyl triethoxysilane.

Radical catalyzed debromination of bromo-alkanes by formate in aqueous solutions via a hydrogen atom transfer mechanism

Shandalov, Elisabetha,Zilbermann, Israel,Maimon, Eric,Nahmani, Yeoshua,Cohen, Haim,Adar, Eilon,Meyerstein, Dan

, p. 989 - 992 (2004)

CO2·- radicals catalyze the dehalogenation of bromo-alkanes by formate via a hydrogen atom transfer mechanism.

A Highly Efficient Copper(II) Complex catalysed Hydrolysis of Methyl Acetate at pH 7.0 and 25 deg C

Chin, Jik,Jubian, Vrej

, p. 839 - 841 (1989)

The turnover time for 2+ (1 mM) catalysed hydrolysis of methyl acetate (1 M) is 23 min at pH 7, 25 deg C.

Selective oxidation of ethane to acetic acid selective oxidation of ethane to acetic acid catalyzed catalyzed by by a c-scorpionate c-scorpionate iron(Ii) iron(ii) complex: Complex: A ahomogeneous vs.vs.heterogeneous comparison

Martins, Luísa M. D. R. S.,Matias, Inês A. S.,Ribeiro, Ana P. C.

, (2020)

The direct, one-pot oxidation of ethane to acetic acid was, for the first time, performed using a C-scorpionate complex anchored onto a magnetic core-shell support, the Fe3O4/TiO2/[FeCl2{κ3 -HC(pz)3}] composite. This catalytic system, where the magnetic catalyst is easily recovered and reused, is highly selective to the acetic acid synthesis. The performed green metrics calculations highlight the “greeness” of the new ethane oxidation procedure.


, p. 192 (1955)

Effect of ammonium perfluorooctanoate on acetylcholinesterase activity and inhibition using MALDI-FTICRMS

Cai, Tingting,Zhang, Li,Wang, Rong,Liang, Chen,Zhang, Yurong,Guo, Yinlong

, p. 80 - 83 (2013)

Ammonium perfluorooctanoate (APFO) is a commercially important compound, but its harm to people's health has raised widespread concern. In the past, the investigations into APFO and its degradation product (perfluorooctanoic acid, PFOA) were all about their effect on indicator compounds in animals and enzyme activities. Here, we provided a new suggestion to investigate the influence of APFO and PFOA. Acetylcholinesterase (AChE) was chosen as research subject to reflect the effect of external perfluorochemicals. We applied matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance mass spectrometry (MALDI-FTICRMS) to detect the activity of AChE rapidly and accurately. On this basis, not only AChE activity but also AChE inhibition was studied carefully. The presence of APFO and PFOA showed obvious increase of AChE activity. Moreover, addition of both APFO and PFOA had enhanced AChE inhibition from organophosphorous (OP) pesticide (irreversible inhibitor). Otherwise, the participation of APFO and PFOA had not increased AChE inhibitions from reversible inhibitor galantamine. These results might provide new insights into the effect of APFO and encourage the deep understanding about effect of APFO on human being.

Oxidative decarboxylation of levulinic acid by cupric oxides

Gong, Yan,Lin, Lu,Shi, Jianbin,Liu, Shijie

, p. 7946 - 7960 (2010)

In this paper, cupric oxides was found to effectively oxidize levulinic acid (LA) and lead to the decarboxylation of levulinic acid to 2-butanone. The effects of cupric oxide dosage, reaction time and initial pH value were investigated in batch experiments and a plausible mechanism was proposed. The results showed that LA decarboxylation over cupric oxides at around 300 °C under acidic conditions produced the highest yield of butanone (67.5%). In order to elucidate the catalytic activity of cupric oxides, XRD, AFM, XPS and H 2-TPR techniques was applied to examine their molecular surfaces and their effects on the reaction process.

Single-pot conversion of methane into acetic acid in the absence of CO and with vanadium catalysts such as amavadine

Reis, Patricia M.,Silva, Jose A. L.,Palavra, Antonio F.,Frausto da Silva, Joao J. R.,Kitamura, Tsugio,Fujiwara, Yuzo,Pombeiro, Armando J. L.

, p. 821 - 823 (2003)

Although its biological function is still unknown, the naturally occurring vanadium complex amavadine may be suitable for industrial applications: This compound (as well as other VIV and VV complexes with N,O and O,O ligands) are shown to act as catalysts for the direct conversion of methane into acetic acid, without requiring CO, under very mild conditions and in high yields (see scheme).

Reactor kinetics studies via process raman spectroscopy, multivariate chemometrics, and kinetics modeling

Assirelli, Melissa,Xu, Weiyin,Chew, Wee

, p. 610 - 621 (2011)

The deployment of in situ analytics for monitoring chemical reactions in process chemistry development and scale-up is facilitated by advanced instrumentation such as Raman spectrometry. Furthermore, greater process understanding can be engendered by coupling in situ Raman data with multivariate chemometrics analyses and kinetics modeling. Such information is important for devising science-based process control strategies along the concept of quality by design (QbD) initiated through the U.S. FDA process analytical technology (PAT) framework. A series of experiments using varied glass reactors, stirring speeds, and isothermal reaction temperatures were designed with acetic anhydride hydrolysis as the model reaction to successfully demonstrate the efficacy of combining in situ Raman spectroscopy, multivariate analyses, and kinetics modeling. Two different Raman measurement methods, using immersion and noncontact probe optics, were tested through a process Raman spectrometer with multiplexing capability. Information-theoretic multivariate chemometrics were applied to elicit pure component spectra and transient concentrations of chemical species, and two differential-algebraic equations modeling approaches were adopted for elucidating chemical and dissolution kinetics information. The variations in reactor vessel type and sizes, stirring speeds, Raman measurements, and kinetics models were compared in this study.

Effect of Pd loading and precursor on the catalytic performance of Pd/WO3-ZrO2 catalysts for selective oxidation of ethylene

Wang, Lixia,Xu, Shuliang,Chu, Wenling,Yang, Weishen

, p. 163 - 166 (2010)

The structure and properties of Pd/WO3-ZrO2 (W/Zr = 0.2) catalysts with different Pd loadings and precursors were investigated. The results indicate that Pd/WO3-ZrO2 prepared from a PdCl2 precursor was optimum for high activity and selectivity. Moreover, ethylene conversion increased with the Pd loading. The structure and nature of the catalysts were characterized using X-ray diffraction, BET N2 adsorption, H2 temperature-programmed reduction and H2 pulse adsorption techniques. The results reveal that the higher catalytic performance of Pd/WO3-ZrO2 prepared from PdCl2 could be related to the formation of polytungstate species and the existence of well-dispersed Pd particles.

Conversion of Formaldehyde to Acetic Acid. Formic Acid as a Stoichiometric CO Substitute

Kaplan, Leonard

, p. 5376 - 5377 (1985)


Dissociative nucleophilic substitution of η2-olefin complexes via a novel η2-vinyl cation inTermediate

Chen, Huiyuan,Harman, W. Dean

, p. 5672 - 5683 (1996)

A series of η2-[Os(NH3)5(vinyl ether)]2+ complexes have been prepared by three independent methods that involve direct coordination of a vinyl ether, alcohol addition to an η2-alkyne complex, or nucleophilic substitution of an η2-vinyl ether species. In the presence of an acid catalyst, the vinyl ether ligand undergoes a novel acid-catalyzed substitution reaction at the α-carbon with a broad range of nucleophiles that includes alcohols, amines, carboxylates, hydrides, silylated enols, nitriles, phosphines, and dialkyl sulfides. These reactions appear to proceed through an elimination-addition process where the first step is loss of an alcohol to form an η2-vinyl cation intermediate. In cases where the α-carbon bears an alkyl group, an η2-vinyl cation species can be isolated and characterized. For example, protonation of [Os(NH3)5(η2-2-methoxypropene)]2+ (3) in neat HOTf allows the characterization of the substitution reaction intermediate η2-[Os(NH3)5(C3H5)]3+ (32), formally a metallocyclopropene that behaves chemically like a vinyl cation. In contrast, when the α-carbon of the vinyl ether bears a hydrogen such as with [Os(NH3)5(η2-ethoxyethene)]2+ (1), the hypothetical vinyl cation intermediate, in absence of a suitable nucleophile, undergoes an intramolecular 1,2-hydrogen shift to yield the Fischer carbyne [(NH3)5Os≡CCH3]3+ (33). Examples of nucleophilic substitution reactions for other types of η2-[Os(NH3)5(olefin)](n+) complexes are also demonstrated.

Dioxygen activation at room temperature during controllable and highly efficient acetaldehyde-to-acetic acid oxidation using a simple iron(III)-acetonitrile complex

Li, Renhong,Kobayashi, Hisayoshi,Yan, Xiaoqing,Fan, Jie

, p. 140 - 146 (2014)

We show that highly efficient acetaldehyde-to-acetic acid oxidation is achieved in a diluted FeCl3-acetonitrile solution (5-100 μM), which proceeds rather rapidly and follows the enzymatic-like Michaelis-Menten kinetics. Interestingly, by adjusting the concentration of FeCl3, we are able to accelerate or shut down the oxidation process conveniently. Based on the catalytic results, spectroscopic evidences and successive DFT calculations, a reactant-initiated, putative mononuclear non-heme iron-oxygen complex, [FeCl(MeCN)4(O)]2+, is proposed as the active oxidizing species to conduct the room temperature reaction with relatively high TOF values (~1.2 s-1). Finally, the putative iron-oxygen complexes are employed to the selective oxidation of benzyl alcohol under ambient conditions.

Structure and characterization of amidase from Rhodococcus sp. N-771: Insight into the molecular mechanism of substrate recognition

Ohtaki, Akashi,Murata, Kensuke,Sato, Yuichi,Noguchi, Keiichi,Miyatake, Hideyuki,Dohmae, Naoshi,Yamada, Kazuhiro,Yohda, Masafumi,Odaka, Masfumi

, p. 184 - 192 (2010)

In this study, we have structurally characterized the amidase of a nitrile-degrading bacterium, Rhodococcus sp. N-771 (RhAmidase). RhAmidase belongs to amidase signature (AS) family, a group of amidase families, and is responsible for the degradation of amides produced from nitriles by nitrile hydratase. Recombinant RhAmidase exists as a dimer of about 107?kDa. RhAmidase can hydrolyze acetamide, propionamide, acrylamide and benzamide with kcat/Km values of 1.14 ± 0.23?mM- 1s- 1, 4.54 ± 0.09?mM- 1s- 1, 0.087 ± 0.02?mM- 1s- 1 and 153.5 ± 7.1?mM- 1s- 1, respectively. The crystal structures of RhAmidase and its inactive mutant complex with benzamide (S195A/benzamide) were determined at resolutions of 2.17?A? and 2.32?A?, respectively. RhAmidase has three domains: an N-terminal α-helical domain, a small domain and a large domain. The N-terminal α-helical domain is not found in other AS family enzymes. This domain is involved in the formation of the dimer structure and, together with the small domain, forms a narrow substrate-binding tunnel. The large domain showed high structural similarities to those of other AS family enzymes. The Ser-cis Ser-Lys catalytic triad is located in the large domain. But the substrate-binding pocket of RhAmidase is relatively narrow, due to the presence of the helix α13 in the small domain. The hydrophobic residues from the small domain are involved in recognizing the substrate. The small domain likely participates in substrate recognition and is related to the difference of substrate specificities among the AS family amidases.

Coenzyme Models. 33. Evidence for Retro-acyloin Condensation as Catalyzed by Thiazolium Ion and Cationic Micelle. Oxidative Trapping of the "Active Aldehyde" Intermediates by Flavin

Shinkai, Seiji,Hara, Youichiro,Manabe, Osamu

, p. 770 - 774 (1983)

N-Hexadecylthiazolium bromide (HxdT) in the CTAB micelle, which is known as an excellent catalytic system for acyloin condensation of aldehydes, catalyzes the reverse reaction (i.e., retro-acyloin condensation) to give aldehydes from α-ketols via the active aldehyde intermediates.The existence of the novel, HxdT-mediated process was proposed on the basis of an experimental discovery that flavin (3-methyltetra-O-acetylriboflavin: MeFl), which is capable of oxidatively trapping the active aldehyde intermediates, is reduced by α-ketols such as acetoin and 3-hydroxy-3-methyl-2-butanone in the micellized HxdT solution.It was further substantiated by detection of acetaldehyde in the final reaction mixture.Based on the diasappearance rate of the absorbance of MeFl, we spectrophotometrically estimated the rate constants for the retro-acyloin condensation.Similarly, biacetyl, the monohydrated species of which is analogous to α-ketol, afforded acetaldehyde and acetic acid in the micellized HxdT solution, the rate constant being greater by factors of 102-103 than those for α-ketols.The relevance of the retro-acyloin condensation to biological systems (e.g., the mechanism of transketolase catalysis) is discussed.

Photoelectrochemistry of Levulinic Acid on Undoped Platinized n-TiO2 Powders

Chum, H. L.,Ratcliff, M.,Posey, F. L.,Turner, J. A.,Nozik, A. J.

, p. 3089 - 3093 (1983)

The photoelectrochemistry of levulinic (4-oxopentanoic) acid, the major product of controlled degradation of cellulose by acids, has been investigated.Since this acid can be present in waste streams of biomass processing, we investigated the photoelectrochemical reactions of this acid on slurries composed of semiconductor/metal particles.The semiconductor investigated was platinized undoped n-TiO2, as anatase, anatase-rutile mixture, or rutile.The effects of the level of platinization, pH, acid concentration, and the semiconductor surface area were investigated.In addition to the decarboxylation reaction leading to methyl ethyl ketone, we have also observed novel cleavages of the C-C backbone leading to propionic acid, acetic acid, acetone, and acetaldehyde as major products.These lower molecular weight carboxylic acids undergo decarboxylation at the slurry diodes to ethane and methane.The organic product distribution is a complex function of the crystallographic phase of n-TiO2 and of the level of metallization of the semiconductor powder.

Formic Acid Promotion of Transition-metal Catalysed Isomerization of Methyl Formate

Cheong, Minserk,Bae, Seong-ho,Lee, Kang B.

, p. 1557 - 1558 (1995)

MeI-HCO2H is an extremely effective promoter/solvent combination for the transition-metal catalysed conversion of methyl formate to acetic acid in the absence of initial carbon monoxide pressure.

Application of band-target entropy minimization to on-line raman monitoring of an organic synthesis. An example of new technology for process analytical technology

Widjaja, Effendi,Ying, Yan Tan,Garland, Marc

, p. 98 - 103 (2007)

The hydrolysis of acetic anhydride to acetic acid in water as solvent was monitored by Raman microscopy. Both static and flow-through configurations were used in the experiments, and various experimental designs, i.e., multiple-experimental runs and multiple-perturbation semibatch mode, were considered. Various spectral data preprocessing was performed and band-target entropy minimization (BTEM) was used in the spectral analysis to recover the pure-component spectra from the multicomponent data. Good and consistent spectral estimates of the solutes acetic anhydride and acetic acid were recovered. In addition, the pure-component spectrum of white-light interference was recovered. Together, these estimates permitted very good estimates of the individual time-dependent signal contributions. Taken together, the present results suggest that the combination of Raman spectroscopy and BTEM has considerable potential for organic syntheses and process analysis. The combination of Raman spectroscopy and BTEM represents another approach for reaction monitoring in process analytical technologies (PAT).

Reaction coordinate analysis for β-diketone cleavage by the non-heme Fe2+-dependent dioxygenase Dke1

Straganz, Grit D.,Nidetzky, Bernd

, p. 12306 - 12314 (2005)

Acetylacetone dioxygenase from Acinetobacter johnsonii(Dke1) utilizes a non-heme Fe2+ cofactor to promote dioxygen-dependent conversion of 2,4-pentanedione (PD) into methylglyoxal and acetate. An oxidative carbon-carbon bond cleavage by Dke1 is triggered from a C-3 peroxidate intermediate that performs an intramolecular nucleophilic attack on the adjacent carbonyl group. But how does Dke1 bring about the initial reduction of dioxygen? To answer this question, we report here a reaction coordinate analysis for the part of the Dke1 catalytic cycle that involves O2 chemistry. A weak visible absorption band (ε ≈ 0.2 mM-1 cm-1) that is characteristic of an enzyme-bound Fe2+-β-keto-enolate complex served as spectroscopic probe of substrate binding and internal catalytic steps. Transient and steady-state kinetic studies reveal that O2-dependent conversion of the chromogenic binary complex is rate-limiting for the overall reaction. Linear free-energy relationship analysis, in which apparent turnover numbers (kcatapp) for enzymatic bond cleavage of a series of substituted β-dicarbonyl substrates were correlated with calculated energies for the highest occupied molecular orbitals of the corresponding β-keto-enolate structures, demonstrates unambiguously that k catapp is governed by the electron-donating ability of the substrate. The case of 2′-hydroxyacetophenone (2′HAP), a completely inactive β-dicarbonyl analogue that has the enol double bond delocalized into the aromatic ring, indicates that dioxygen reduction and C-O bond formation cannot be decoupled and therefore take place in one single kinetic step.

Photophysics of Perylene Diimide Dianions and Their Application in Photoredox Catalysis

Li, Han,Wenger, Oliver S.

supporting information, (2021/12/23)

The two-electron reduced forms of perylene diimides (PDIs) are luminescent closed-shell species whose photochemical properties seem underexplored. Our proof-of-concept study demonstrates that straightforward (single) excitation of PDI dianions with green

The influence of different carbonate ligands on the hydrolytic stability and reduction of platinum(

Chen, Shu,Deng, Zhiqin,Ng, Ka-Yan,Tse, Man-Kit,Yao, Houzong,Zhou, Qiyuan,Zhu, Guangyu

supporting information, p. 885 - 897 (2022/02/01)

Pt(iv) complexes bearing axial carbonate linkages have drawn much attention recently. A synthetic method behind this allows the hydroxyl group of bioactive ligands to be attached to the available hydroxyl group of Pt(iv) complexes, and the rapid release of free drugs is achieved after the reduction of carbonate-linked Pt(iv) complexes. Further understanding on the properties of Pt(iv) carbonates such as hydrolytic stability and reduction profiles, however, is hindered by limited research. Herein, six mono-carbonated Pt(iv) complexes in which the carbonate axial ligands possess various electron-withdrawing powers were synthesized, and the corresponding mono-carboxylated analogues were also prepared as references to highlight the different properties. The influence of the coordination environment towards the hydrolysis and reduction rate of Pt(iv) carbonates and carboxylates was explored. The mono-carbonated Pt(iv) complexes are both less stable and reduced faster than the corresponding mono-carboxylated ones. Moreover, the hydrolysis and reduction profiles are dependent not only on the electron-withdrawing ability of the carbonates but also on the nature of the opposite axial ligands. Besides, the exploration of the hydrolytic pathway for Pt(iv) carbonates suggests that the process proceeds by an attack of OH? on the carbonyl carbon, followed by elimination, which is different from that of Pt(iv) carboxylates. This study provides some information on the influence of axial carbonate ligands with different electron-withdrawing abilities on the properties of the Pt(iv) center, which may inspire new thoughts on the design of “multi-action” Pt(iv) prodrugs.

2-(4-Nitrophenyl)-1H-indolyl-3-methyl Chromophore: A Versatile Photocage that Responds to Visible-light One-photon and Near-infrared-light Two-photon Excitations

Abe, Manabu,Guo, Runzhao,Hamao, Kozue,Lin, Qianghua,Takagi, Ryukichi

supporting information, p. 153 - 156 (2022/02/14)

Due to cell damage caused by UV light, photoremovable protecting groups (PPGs) that are removed using visible or near-infrared light are attracting attention. A 2-(4-nitrophenyl)- 1H-indolyl-3-methyl chromophore (NPIM) was synthesized as a novel PPG. Various compounds were caged using this PPG and uncaged using visible or near-infrared light. Low cytotoxicity of NPIM indicates that it may be applied in physiological studies.

Process route upstream and downstream products

Process route







acetic acid

acetic acid

propionic acid

propionic acid

Conditions Yield
beim Nitrieren;




3-methoxybutanoic acid

3-methoxybutanoic acid

acetic acid

acetic acid

Conditions Yield
bei der Ozonolyse;


palmitic acid

palmitic acid

acetic acid

acetic acid

Conditions Yield
With chromic acid;


vinyl triacetoxy silane

vinyl triacetoxy silane





acetic acid

acetic acid







Conditions Yield
With water; for 80h; Product distribution; several condition investigated;
3.5-Dinitro-aspirin, (O-Acetyl-3.5-dinitro-salicylsaeure)

3.5-Dinitro-aspirin, (O-Acetyl-3.5-dinitro-salicylsaeure)

3,5-dinitrosalicylic acid

3,5-dinitrosalicylic acid

acetic acid

acetic acid

Conditions Yield
With water; In acetonitrile; at 25 ℃; Rate constant;


acetic acid

acetic acid



Conditions Yield
With hydrogenchloride; In water; at 30 ℃; Rate constant; hydrolysis;
With cetyltrimethylammonim bromide; at 102.9 ℃; Mechanism; borate buffer pH 9.0; inhibition by var. salts added;
With Rhodococcus erythropolis TA37 acylamidase; water; tris hydrochloride; at 37 ℃; for 0.333333h; pH=7.5; Kinetics; Enzymatic reaction;
4-nitrophenol acetate

4-nitrophenol acetate

acetic acid

acetic acid

Conditions Yield
With (ZnII-(1,5,9-triazacyclododecane)(OH))3*(ClO4)3; water; at 25 ℃; Rate constant; pH 8.2, I = 0.10 (NaClO4);
With pH 8.2 phosphate buffer; water; β-DMCD bearing imidazolylethyl group; at 25 ℃; Rate constant; pH dependence of kcat is determined;
With poly<1-methyl-3-(2-hydroxyethyl)imidazolium bromide>; In ethanol; at 23.9 ℃; Rate constant; var. pH;
With hydrogenchloride; water; In water; at 25 ℃; Thermodynamic data; ΔGtrΘ, ΔHtrΘ, ΔStrΘ, ΔCpΘ of transfer;
With water; various imidazoles; at 25 ℃; Rate constant;
With MES-buffer; Alkyl-pyridine*Cu(2+); at 35 ℃; Rate constant; Mechanism; Equilibrium constant; pH 6.25;
cetyldimethyl-(2-hydroxyiminophenethy..; In ethanol; water; at 30 ℃; Rate constant; variuos catalysts, pH=8.0-8.8;
With disodium hydrogenphosphate; sodium dihydrogenphosphate; water; acetylcholinesterase; at 25 ℃; Rate constant; pH 7.50; isotope effect 0.992; further reagents;
With 1H-imidazole; water; In ethanol; at 25 ℃; Mechanism; Kinetics; phosphate buffer (pH=8.05);
With water; In 1,4-dioxane; at 25 ℃; Rate constant;
With 2-aminopyridine; water; at 30 ℃; Rate constant; Mechanism; other aminopyridines and aniline;
With phosphate buffer; H-His-Ser-Asp-Ala-OH; In 1,4-dioxane; at 25 ℃; Rate constant;
Z-Leu-His; at 25 ℃; Rate constant; Mechanism; pH=7.30, 0.02M phosphate buffer; further catalyst; effect of surfactants;
With buffer solution; pilocarpine hydrochloride; In water; acetonitrile; at 24.9 ℃; Rate constant; other catalysts, var. pH-values;
With N,N',N'',N'''-tetrakis-<10-decyl>-3,10,21,28-tetraoxo-2,11,20,29-tetra-aza<>paracyclophane tetrachloride; In ethanol; water; at 30 ℃; Rate constant; other catalyst (three isomers containing two imidazolyl groups on adjacent and opposite alkyl chains); catalytic activity and substrate selectivity of both paracyclophanes compared; pH dependency of the substrate-binding ability of the cyclophanes;
With sodium glycocholic acid; water; at 37.4 ℃; Rate constant; var. concentration of other bile salts; var. pH; phosphate buffer;
With erythromycin A-hydrolyse prod.; water; In 1,4-dioxane; at 20 ℃; Rate constant; pH 11.972;
With water; cyclo-L-histydyl-L-histydyl; In 1,4-dioxane; at 20 ℃; Thermodynamic data; Kinetics; other p-nitrophenyl esters, var. catalyst and pH, ΔH, ΔS, ΔG;
With hydroxide; at 23 ℃; Mechanism; pH 9.0; 15N kinetic isotope effect; also reaction with phenol;
With Tris buffer; zinc(II) perchlorate; podant1 + Zn(ClO4)2; In water; acetonitrile; Rate constant; with other endodentate tripodand-Zn(2+)-complexes , variation of pH;
With borate buffer; hydroxide; In ethanol; water; at 25 ℃; Rate constant;
With water; In dimethyl sulfoxide; at 35 ℃; Kinetics; Thermodynamic data; pH=13.12; ΔH(excit.); -ΔS(excit.); different substrate concentrations, ratios of solvents and temperature;
apo-Mb semisynthetic enzyme; In water; at 25 ℃; Rate constant; Mechanism; buffer : 0.05 M Tris, pH 8;
With alkaline solution; In water; acetonitrile; at 24.9 - 25.1 ℃; Rate constant; carbonate buffer pH 10.70;
With borate buffer; water; C18H22F17N2O2(1+); In acetonitrile; at 30 ℃; Rate constant; var. further catalyst, catalyst concn.;
With sodium hydroxide; poly(trimethylvinylbenzylammonium chloride); at 25 ℃; Thermodynamic data; without PMVA and also with sodium poly(styrenesulfonate); ΔG(excit.), ΔH(excit.), ΔS(excit.);
With 1-methyl-1H-imidazole; water; In dichloromethane; also in the presence of NO and protoheme dimethyl ester;
With o-(N,N-dimethylaminomethyl)benzyl alcohol; water; at 25 ℃; Rate constant; var. ionic strength and pH, other tertiary amine as catalysts;
With Tris-HCl buffer; water; In acetonitrile; Rate constant; Kinetics; Thermodynamic data; IgG and IgM monoclonal antibodies as catalysts (antibody KD2-1 - KD2-260); var. temp., var. pH; ΔH(excit.), ΔG(excit.), ΔS(excit.);
With cetyltrimethylammonim bromide; 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine; In water; at 25 ℃; Kinetics; Tris buffer solution (pH=8.0); the effect of lecithin dispersed by surfactants on the rate hydrolysis;
α-chymotrypsin; In acetonitrile; at 10 - 57 ℃; Kinetics; Mechanism; ΔH(excit.), ΔS(excit.), ΔF(excit.), heat and pressure inactivation of α-chymotrypsin;
With phosphate buffer; N-(tert-butoxycarbonyl)-L-histidine methyl ester; In water; N,N-dimethyl-formamide; at 25 ℃; Rate constant; imidazole and other histidine-containing linear and cyclic peptides;
With 1-methyl-1H-imidazole; 2-(cyclohexylamino)ethanesulfonic acid; In acetonitrile; at 27 ℃; Rate constant; Mechanism; other p-nitrophenyl esters; other methyl-substituted imidazoles; solvent isotope effects;
With cetyltrimethylammonim bromide; (2S)-N-decanoyl-2-amino-3-(1H-imidazol-4-yl)propionic acid; at 25 ℃; Rate constant; other catalytic system; deacylation effect of bifunctional comicellar catalyst; pH 7.30;
With bis(2-ethylhexyl) sulfosuccinate; water; at 15 ℃; under 225018 Torr; Kinetics; examination of effects of pressure;
With water; at 24 ℃; Kinetics;
With 6-deoxy-6-(L-histydylamino)-β-cyclodextrin; In water; at 25 ℃; Rate constant; phosphate buffer pH 7.8; other cyclodextrin;
With Carbonate buffer; alpha cyclodextrin; In water; dimethyl sulfoxide; at 25 ℃; Rate constant; various solvents; also with β-cyclodextrin;
With dm-3 phosphate buffer; at 25 ℃; Rate constant; pH 11.60; also in the presence of cyclodextrins at var conc. and var. nucleophiles;
With water; In methanol; at 25 ℃; Thermodynamic data; Rate constant; the role of the ultrasonic irradiation; ΔH(excit.), ΔS(excit.) and ΔG(excit.) datas in the presence and absence of ultrasound; various cavitatingases; pH dependence; effect of ionic strength, the role of supercritical water;
With sodium nitrate; zinc; In acetonitrile; at 25 ℃; Rate constant; var. catalysts;
With 1H-imidazole; hydrogenchloride; potassium chloride; water; In acetonitrile; at 25.1 ℃; Rate constant; var. pH, conc.;
With dmap; phosphate buffer; cetyltrimethylammonim bromide; In cyclohexane; butan-1-ol; at 25 ℃; Rate constant; other dialkylaminopyridines; var. microemulsion's composition;
With phosphate buffer; Thr-Ala-Ser-His-Asp; In 1,4-dioxane; at 28 ℃; Rate constant; other reaction partner system;
With octa(dimethylaminopropyl)resorcin<4>arene; water; at 25 ℃; Rate constant; Mechanism; other carboxylic acid 4-nitrophenyl esters;
With hydrogenchloride; poly(Asp-Leu-His-Leu-Ser-Leu); 2-amino-2-hydroxymethyl-1,3-propanediol; In ethanol; at 25 ℃; Kinetics; Thermodynamic data; also with Asp-Leu-His-Leu-Ser-Leu hexamer; ΔE(excit.); ΔH(excit.); ΔF(excit.); ΔS(excit.); var. temp.;
With SULFAMIDE; carbonic anhydrase II; In water; acetonitrile; at 25 ℃; Rate constant; other reagents;
With pH 11.6 phosphate buffer; cetyltrimethylammonim bromide; sodium bromide; In acetonitrile; at 25 ℃; Rate constant;
With borate buffer; TMA-quaternized butyl methacrylate latex; water; at 30 ℃; Rate constant; also in the presense of other trimethylamine or tributylamine quaternized latexes;
With pH=5.1 buffer; polypeptide MN-42; In water; acetonitrile; at 16.9 ℃; Rate constant; other polypetides vith var. amino acids sequences;
With 1H-imidazole; water; In acetonitrile; at 5 - 35 ℃; Further Variations:; Temperatures; Solvents; Kinetics; Activation energy;
With 2-aminobenzimidazole grafted on polymer; potassium chloride; tris hydrochloride; In ethanol; at 30.85 - 49.85 ℃; pH=7.5; Further Variations:; Reagents; Temperatures; Kinetics; Thermodynamic data;
With acetate buffer; JNIIHR polypeptide; In acetonitrile; at 16.85 ℃; pH=5.1; Further Variations:; Reagents; Kinetics;
With cellulose acetate esterase from Neisseria sicca SB; tris hydrochloride; In water; at 30 ℃; pH=8.0; Enzyme kinetics;
With MES buffer; water; 1-Dodecyl-4-[1-(hydroxyimino)ethyl]pyridinium bromide; at 25 ℃; pH=7.2; Further Variations:; Reagents; Kinetics;
With dodecyltrimethylammonium bromide; fipronilβ-cyclodextrin; at 25 ℃; Further Variations:; Reagents; Kinetics; Alkaline hydrolysis;
With iron (III) chelate of 1,2-bis(2-hydroxybenzamido)ethane; water; In methanol; at 26.5 ℃; Further Variations:; Reagents; pH-values; Kinetics;
With PEG-8000; Tris buffer; trypsin; In acetonitrile; at 25 ℃; pH=7.7; Further Variations:; Reagents; Enzyme kinetics;
With human carbonic anhydrase I EC; Tris buffer; In water; acetonitrile; at 25 ℃; pH=7.8; Further Variations:; Reagents; Enzyme kinetics;
With sodium hydroxide; 2,2,4-trimethylpentane; sodium docusate; at 25 ℃; Further Variations:; Reagents; pH-values; Kinetics;
With AcAPLEPEYPGDNATPEQMHQYAHQLRRYINMLCONH2; In acetate buffer; at 16.85 ℃; pH=5.1; Further Variations:; pH-values; Reagents; Kinetics;
human serum albumin; In phosphate buffer; at 25 ℃; pH=7.4; Further Variations:; Catalysts; Temperatures; Activation energy;
With sodium phosphate buffer; Aspergillus niger ZD11 pyrethroid hydrolase; In acetonitrile; at 30 ℃; pH=6.8; Enzyme kinetics;
With sodium phosphate buffer; Klebsiella sp. ZD112 pyrethroid-hydrolyzing esterase; In acetonitrile; at 30 ℃; pH=7.0; Enzyme kinetics;
With Leu29Pro Pseudomonas fluorescens esterase; N,N-bis(2-hydroxyethyl)-2-aminoethanesulfonic acid buffer; at 25 ℃; pH=7.2; Further Variations:; Reagents; Enzyme kinetics;
With sodium acetate buffer; modified Argopore-NH2; In water; acetonitrile; pH=5.0; Further Variations:; Reagents; Kinetics; Product distribution;
With water; αC2DTC; In various solvent(s); at 25 ℃; for 0.2h; pH=9.0; Further Variations:; Catalysts; pH-values; reaction times; Kinetics;
With esterase antibody 522C2; In 1,4-dioxane; at 30 ℃; pH=7.5; Enzyme kinetics;
With water; dinuclear Zn; In acetonitrile; at 25 ℃; pH=9.0; Further Variations:; pH-values; Kinetics;
With 4-methyl-1H-imidazole; water; at 16.84 ℃; pH=5.1; Kinetics;
With potassium chloride; water; at 25 ℃; pH=12.7; Further Variations:; pH-values; Reagents; reagents ratios; Kinetics;
With aq. bis-Tris buffer; [N-(3-(MeO)2CH-benzoyl)-1-Bn-L-histidyl]hydrazine cyclodimer; at 25 ℃; pH=6.20; Further Variations:; pH-values; Reagents; Kinetics;
With Burkholderia xenovorans LB400 BphD; In phosphate buffer; at 25 ℃; pH=7.0; Further Variations:; Reagents; Enzyme kinetics;
With sodium hydroxide; cetyltrimethylammonim bromide; at 25 ℃; Further Variations:; Reagents; Kinetics;
With 1H-imidazole; water; In ethanol; Temperature; Kinetics; Activation energy; Mechanism;
With Zn(5,11,17,23-tetra-tert-butyl-25,27-bis[2-[N-(2-hydroxybenzylidene)amino]ethoxy]-26,28-dihydroxycalix[4]arene); water; In acetonitrile; at 25 ℃; pH=8.27; pH-value; Kinetics;
With 6-aminohexanoate cyclic dimer hydrolase Arthrobacter sp.; at 30 ℃; pH=7; aq. phosphate buffer; Enzymatic reaction;
With Acinetobacter johnsonii dioxygenase Dke1; at 25 ℃; pH=7.5; Reagent/catalyst; Time; Kinetics; aq. buffer; Enzymatic reaction;
With human intestinal carboxylesterase; pH=7.4; Reagent/catalyst; Kinetics; aq. buffer; Enzymatic reaction;
With water; Fe2O3-Cys-Lys nanocomplex; at 37 ℃; for 48h; pH=7; Conversion of starting material;
With EstEH112 esterase; water; at 25 ℃; pH=8; GTA buffer; Enzymatic reaction;
With potassium chloride; water; 1,6-bis(N-hexadecyl-N,N-dimethylammonium)hexane dibromide; sodium hydroxide; at 25 ℃; Reagent/catalyst; Kinetics;
With sodium nitrate; C18H44Cu2N6O2(2+)*2ClO4(1-); water; In acetonitrile; for 25h; pH=8.8; Reagent/catalyst; Time; pH-value; Kinetics; Catalytic behavior;
With Pseudomonas fluorescens esterase; In aq. buffer; at 23 ℃; pH=7.2; Reagent/catalyst; Kinetics; Enzymatic reaction;
With Candida antarctica lipase B; In aq. phosphate buffer; at 20 ℃; pH=7; Reagent/catalyst; Kinetics; Enzymatic reaction;
With carboxylesterase EstSt7 from Sulfolobus tokodaii strain 7; water; In ethanol; at 80 ℃; pH=9; Kinetics; Enzymatic reaction;
With lipase from Candida rugosa; In aq. phosphate buffer; pH=7; pH-value; Enzymatic reaction;
With recombinant esterase from Rhizomucor miehei; In isopropyl alcohol; at 50 ℃; for 0.166667h; pH=7.5; Catalytic behavior; Kinetics; Enzymatic reaction;
With lipase PS from Burkholderia cepacia, immobilized in calcium carbonate microcapsule; In acetone; at 25 ℃; pH=7.0; Catalytic behavior; Enzymatic reaction;
With SLMKDTDSEE EIREAFRVFD KDGNGYISAA ELRHVMTNLG EKLTDEEVDE MIREADIDGD GQVNYEEFVQ HMTAK*; water; sodium chloride; calcium chloride; N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid; In acetonitrile; pH=7.5; Reagent/catalyst; Kinetics; Enzymatic reaction;
With Burkholderia species lipoprotein lipase; C35H61NO17; water; In aq. phosphate buffer; at 25 ℃; pH=7.0; Kinetics; Catalytic behavior; Enzymatic reaction;
With Dactylosporangium aurantiacum subsp. Hamdenensis NRRL 18085 esterase WDEst17; water; In acetonitrile; at 40 ℃; pH=8.5; pH-value; Temperature; Solvent; Reagent/catalyst; Catalytic behavior; Kinetics; Enzymatic reaction;
With human carbonic anhydrase; In water; pH=7.4; Enzymatic reaction;
With C20H18N6; water; In aq. phosphate buffer; at 25 ℃; pH=7.6; Reagent/catalyst; Solvent; Kinetics; Irradiation; Darkness;
With Dactylosporangium aurantiacum esterase WDEst9; In aq. phosphate buffer; ethanol; acetonitrile; at 35 ℃; for 0.0833333h; pH=7.5; Catalytic behavior; Enzymatic reaction;
With water; In toluene; at 25 ℃; Kinetics; Enzymatic reaction;
In aq. buffer; at 25 ℃; pH=9;
With water; Rhizopus oryzae ZAC3 lipase; In aq. phosphate buffer; isopropyl alcohol; pH=8; Enzymatic reaction;


formic acid

formic acid





acetic acid

acetic acid





Conditions Yield
With ozone; hydrazine; at 22.9 ℃; for 0.75h; Product distribution; different reagent concentrations, times;
p-Nitrophenyl laurate

p-Nitrophenyl laurate

acetic acid

acetic acid

Conditions Yield
With cetyltrimethylammonim bromide; N-decanoyl-L-histidine; at 25 ℃; Rate constant; other catalytic system; deacylation effect of bifunctional comicellar catalyst; pH 7.30;
p-nitrophenyl hexanoate

p-nitrophenyl hexanoate

acetic acid

acetic acid

Conditions Yield
With cetyltrimethylammonim bromide; N-decanoyl-L-histidine; at 25 ℃; Rate constant; other catalytic system; deacylation effect of bifunctional comicellar catalyst; pH 7.30;

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