589-75-3Relevant academic research and scientific papers
Kinetic Study of Liquid-Phase Esterification with Sulfonic Acid Cation-Exchange Resin of the Macroreticular Type. II. Solvent Effects on Resin Catalysis
Shimizu, Shoichi,Hirai, Choichiro
, p. 1975 - 1980 (1987)
The rates of the esterification of octanoic acid with 1-butanol catalyzed by macroreticular sulfonated ion-exchange resin in the presence of various organic solvents and water were measured by the use of a batch reactor.The solvent effects on the rate were investigated by applying the heterogeneous-pseudohomogeneous reaction mechanism.From these results, it was found that the effects can be quantitatively estimated by means of the magnitude of the equilibrium constants, K(S)sol, for the solvent-separated ion-pair formations, which are due to the interaction of the sulfo groups in the resin with the solvents.The correlations of the K(S)sol value with the physical properties, μ end ε; the solvatochromic parameters ?*, α, and β, and Gutmann's parameters, ANE and DNB, have been examined by using linear regession analysis methods.The results of the correlations in which the protic solvents have been excluded suggest that the positions of the equilibria of solvent-separated ion-pair formations depend mainly on the electron-donor property of the solvents; that is to say, the solvents with a strong donor property diminish the number of un-ionized sulfo groups which act as catalytic species for the heterogeneous reaction.
Kinetic Study of Liquid-Phase Esterification with Sulfonic Acid Cation-Exchange Resin of the Macroreticular Type. I. Heterogeneous-Pseudohomogeneous Resin Catalysis
Shimizu, Shoichi,Hirai, Choichiro
, p. 7 - 12 (1986)
The rates of the esterification of octanoic acid with 1-butanol catalyzed by macroreticular sulfonated ion-exchange resin were measured by teh use of a batch reactor.The effects on the rate were investigated for variations in the amount of the catalyst, the temperature, and the reactant alcohol concentrations as well as those of water and butyl octanoate.From these data, it is considered that alcohol and water solvate the matrix-bound sulfo groups, and so this esterification system consists of a heterogeneous reaction catalyzed by un-ionozed sulfo groups and a pseudo-homogeneous reaction catalyzed by solvated protons; in other words, catalysis by sulfonic acid resin is both heterogeneous and pseudo-homogeneous in liquid-phase esterification.
Immobilization of lipase in organic solvent in the presence of fatty acid additives
Ozturk, Taylan K.,Kilinc, Ali
, p. 214 - 218 (2010)
In this study porcine pancreatic lipase (PPL) was covalently immobilized on cross-linked polyvinyl alcohol (PVA) in organic media in the presence of fatty acid additives in order to improve its immobilized activity. The effects of fatty acid additions to the immobilization media were investigated choosing tributyrin hydrolysis in water and ester synthesis by immobilized PPL in n-hexane. Various fatty acids which are also the substrates of lipases in esterification reactions were used as active site protecting agents during the immobilization process in an organic solvent. The obtained results showed that covalent immobilization carried out in the presence of fatty acids as protective ligands improved the hydrolytic and esterification activity of immobilized enzyme. A remarkable increase in activity of the immobilized PPL was obtained when octanoic acid was used as an additive and the hydrolytic activity was increased from 5.2 to 19.2 μmol min-1 mg-1 as compared to the non-additive immobilization method. With the increase of hydrolytic activity of immobilized lipase in the presence of octanoic acid, in an analogous manner, the rate of esterification for the synthesis of butyl octanoate was also increased from 7.3 to 26.3 μmol min-1 g-1 immobilized protein using controlled thermodynamic water activities with saturated salt solutions. In addition, the immobilized PPL activity was maintained at levels representing 63% of its original activity value after 5 repeated uses. The proposed method could be adopted for a wide variety of other enzymes which have highly soluble substrates in organic solvent such as other lipases and esterases.
Carboxylic Acid Reductase Can Catalyze Ester Synthesis in Aqueous Environments
Pongpamorn, Pornkanok,Kiattisewee, Cholpisit,Kittipanukul, Narongyot,Jaroensuk, Juthamas,Trisrivirat, Duangthip,Maenpuen, Somchart,Chaiyen, Pimchai
supporting information, p. 5749 - 5753 (2021/02/01)
Most of the well-known enzymes catalyzing esterification require the minimization of water or activated substrates for activity. This work reports a new reaction catalyzed by carboxylic acid reductase (CAR), an enzyme known to transform a broad spectrum of carboxylic acids into aldehydes, with the use of ATP, Mg2+, and NADPH as co-substrates. When NADPH was replaced by a nucleophilic alcohol, CAR from Mycobacterium marinum can catalyze esterification under aqueous conditions at room temperature. Addition of imidazole, especially at pH 10.0, significantly enhanced ester production. In comparison to other esterification enzymes such as acyltransferase and lipase, CAR gave higher esterification yields in direct esterification under aqueous conditions. The scalability of CAR catalyzed esterification was demonstrated for the synthesis of cinoxate, an active ingredient in sunscreen. The CAR esterification offers a new method for green esterification under high water content conditions.
1,3-Dibromo-5,5-dimethylhydantoin as a Precatalyst for Activation of Carbonyl Functionality
?ebular, Klara,Bo?i?, Bojan ?.,Stavber, Stojan
, (2019/08/01)
Activation of carbonyl moiety is one of the most rudimentary approaches in organic synthesis and is crucial for a plethora of industrial-scale condensation reactions. In esterification and aldol condensation, which represent two of the most important reactions, the susceptibility of the carbonyl group to nucleophile attack allows the construction of a variety of useful organic compounds. In this context, there is a constant need for development of and improvement in the methods for addition-elimination reactions via activation of carbonyl functionality. In this paper, an advanced methodology for the direct esterification of carboxylic acids and alcohols, and for aldol condensation of aldehydes using widely available, inexpensive, and metal-free 1,3-dibromo-5,5-dimethylhydantoin under neat reaction conditions is reported. The method is air- and moisture-tolerant, allowing simple synthetic and isolation procedures for both reactions presented in this paper. The reaction pathway for esterification is proposed and a scale-up of certain industrially important derivatives is performed.
Development and Validation of a Novel Free Fatty Acid Butyl Ester Gas Chromatography Method for the Determination of Free Fatty Acids in Dairy Products
Mannion, David T.,Furey, Ambrose,Kilcawley, Kieran N.
, p. 499 - 506 (2019/01/08)
Accurate quantification of free fatty acids in dairy products is important for both product quality control and legislative purposes. In this study, a novel fatty acid butyl ester method was developed, where extracted free fatty acids are converted to butyl esters prior to gas chromatography with flame ionization detection. The method was comprehensively validated to establish linearity (20-700 mg/L; R2 > 0.9964), limits of detection (5-8 mg/L), limits of quantification (15-20 mg/L), accuracy (1.6-5.4% relative error), interday precision (4.4-5.3% relative standard deviation), and intraday precision (0.9-5.6% relative standard deviation) for each individual free fatty acid. A total of 17 dairy samples were analyzed, covering diverse sample matrices, fat content, and degrees of lipolysis. The method was compared to direct on-column injection and fatty acid methyl ester methods and overcomes limitations associated with these methods, such as either column-phase absorption or deterioration, accurate quantification of short-chain free fatty acids, and underestimation of polyunsaturated free fatty acid.
Esterification of aryl/alkyl acids catalysed by n-bromosuccinimide under mild reaction conditions
?ebular, Klara,Bo?i?, Bojan ?.,Stavber, Stojan
, (2018/09/10)
N-halosuccinimides (NXSs) are well-known to be convenient, easily manipulable and low-priced halogenation reagents in organic synthesis. In the present work, N-bromosuccinimide (NBS) has been promoted as the most efficient and selective catalyst among the NXSs in the reaction of direct esterification of aryl and alkyl carboxylic acids. Comprehensive esterification of substituted benzoic acids, mono-, di- and tri-carboxy alkyl derivatives has been performed under neat reaction conditions. The method is metal-free, air- and moisture-tolerant, allowing for a simple synthetic and isolation procedure as well as the large-scale synthesis of aromatic and alkyl esters with yields up to 100%. Protocol for the recycling of the catalyst has been proposed.
A simple route to 1,4-addition reactions by Co-catalyzed reductive coupling of organic tosylates and triflates with activated alkenes
Hsieh, Jen-Chieh,Chu, Yi-Hua,Muralirajan, Krishnamoorthy,Cheng, Chien-Hong
, p. 11584 - 11587 (2017/10/27)
An efficient Co-catalyzed 1,4-addition reaction of alkyl/aryl triflates and tosylates with activated alkenes is described. In this reaction, an air-stable cobalt(ii) complex, a mild reducing agent Zn and a simple proton source (H2O) are used. A radical mechanism for the addition of alkyl tosylates to activated alkenes is likely involved.
Performance in synthetic applications of a yeast surface display-based biocatalyst
Eby,Peretti
, p. 30425 - 30432 (2015/04/22)
This work demonstrates the effectiveness of yeast surface display (YSD) as a scaffold for biocatalysts in hydrophobic, non-aqueous environments. Two lipases, Candida antarctica lipase B (CalB) and Photobacterium lipolyticum sp. M37 lipase (M37L), were immobilized independently by surface display on Saccharomyces cerevisiae. The two YSD biocatalysts were employed to synthesize esters of butanol and saturated fatty acids of varying length (8 to 16 carbons) in heptane. Effects of fatty acid chain length and temperature on the esterification reaction were examined. The YSD catalysts synthesized butyl decanoate in 10 repeated batches with little loss in activity. Compared to a commercial immobilized lipase (Novozym 435), the activity of both YSD lipases was lower on a mass loading basis, but higher when normalized on estimates of protein loading. Initial-rate kinetics of the butyl decanoate reaction were measured for the CalB-displaying yeast. Kinetics and apparent activity of M37L in the multi-batch experiments depend heavily on water concentration; kinetics for M37L could not be elucidated with initial-rate methods. The difference between CalB and M37L in water requirements illustrates a critical parameter for optimization of lipase activity in non-aqueous environments. The activity of both lipases in a completely hydrophobic environment is a step towards more economical biocatalysis of industrial esterification.
Characterization, performance, and applications of a yeast surface display-based biocatalyst
Eby,Peretti
, p. 19166 - 19175 (2015/06/15)
This work demonstrates the efficacy and cost effectiveness of yeast surface display (YSD) as a method for producing and purifying enzyme catalysts. Lipase B from Candida antarctica (CalB) and lipase from Photobacterium lipolyticum sp. M37 (M37L) were individually displayed on the surface of yeasts via fusion with alpha-agglutinin. The enzyme is produced, purified, and immobilized in a single step. The population expressing the enzyme was quantified by flow cytometry. After lyophilization, the hydrolytic activity of the biocatalyst was assayed with p-nitrophenyl butyrate and p-nitrophenyl palmitate substrates. Esterification reactions involving octanoic acid and either butanol or octanol were used to evaluate esterification activity. The lyophilized YSD biocatalyst hydrolytic activity matched or exceeded commercial lipase (Novozym 435) immobilized on acrylic resin at equal catalyst loading, and achieved esterification levels 10-50% that of Novozyme 435. Factoring in the cost of production, the YSD biocatalyst represents a considerable savings over traditionally prepared and purchased enzyme catalysts. This promises to significantly expand the catalytic applications of immobilized lipases, and immobilized enzymes more generally, in commercial processes. This journal is
