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Solvent-free System (solvent-free + system)
Selected AbstractsInfluence of methanol on the enantioresolution of antihistamines with carboxymethyl-,-cyclodextrin in capillary electrophoresisELECTROPHORESIS, Issue 16 2004Ann Van Eeckhaut Abstract According to the model of Wren and Rowe, the separation between two enantiomers in capillary electrophoresis (CE) decreases if an organic modifier is added to the run buffer containing a neutral cyclodextrin (CD) in a concentration below its optimal value in a solvent-free system. In previous work, however, it was observed that the addition of methanol to the background electrolyte (BGE) containing not charged carboxymethyl-,-CD in a concentration below its optimal value, increased the enantioresolution of dimetindene maleate. The enantioresolution decreased when other organic modifiers (ethanol, isopropanol or acetonitrile) were added and/or when other neutral (,-CD, hydroxypropyl-,-CD) or chargeable (carboxyethyl-,- and succinyl-,-CD) CDs were used. In this CE study further attempts are made to elucidate the observed phenomena through investigating other basic drugs. The effect of organic modifier and CD concentration on the enantioseparation was studied by means of central composite designs. It is shown that obtaining this increase in enantioresolution depends upon the type of CD, the type of organic modifier, and the structure of the analytes. It was also observed that small differences in the structure of the analytes or the CD could have an influence on the enantioresolution. The addition of methanol also resulted in different effects on the resolution of closely related analytes. [source] Influence of silica gel in production of diacylglycerol via enzymatic glycerolysis of palm oleinEUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY, Issue 6 2009Chiou Moi Yeoh Abstract Enzymatic glycerolysis was explored in this paper for the production of diacylglycerol (DAG) oils from palm olein. Three commercial enzymes, Lipozyme TL,IM, Lipozyme RM,IM and Novozym 435 were used for their ability to synthesize DAG in a solvent-free system. Novozym 435 was found to be the more effective enzyme, resulting in a high DAG production even in the absence of an adsorbent such as silica gel. The yields of DAG were between 43 and 50,wt-%. Lipozyme TL,IM and RM,IM, being supported on hydrophilic materials, require an adsorbent to allow slow release of glycerol for reaction with the enzyme and oil. In the absence of silica, no reaction was observed. The success of the reaction is therefore very dependent on the amount of silica used. The yields of DAG using Lipozyme TL,IM and RM,IM were 52 and 45,wt-%, respectively. In addition, the degree of reduction in tocopherols and tocotrienols appeared correlated with the efficacy of the glycerolysis reaction. Changes in the slip melting points and solid fat contents of the products are indicative of the reaction occurring. [source] Lipase-catalyzed ethanolysis of soybean oil in a solvent-free system using central composite design and response surface methodologyJOURNAL OF CHEMICAL TECHNOLOGY & BIOTECHNOLOGY, Issue 6 2008Rafael Costa Rodrigues Abstract BACKGROUND: In this work we describe the synthesis of ethyl esters, commonly known as biodiesel, using refined soybean oil and ethanol in a solvent-free system catalyzed by lipase from Thermomyces lanuginosus. Central composite design and response surface methodology (RSM) were employed to optimize the biodiesel synthesis parameters, which were: reaction time, temperature, substrate molar ratio, enzyme content, and added water, measured as percentage of yield conversion. RESULTS: The optimal conditions obtained were: temperature, 31.5 °C; reaction time, 7 h; substrate molar ratio, 7.5:1 ethanol:soybean oil; enzyme content, 15% (g enzyme g,1 oil); added water, 4% (g water g,1 oil). The experimental yield conversion obtained under these conditions was 96%, which is very close to the maximum predicted value of 94.4%. The reaction time-course at the optimal values indicated that 5 h was necessary to obtain high yield conversions. CONCLUSION: A high yield conversion was obtained under the optimized conditions, with relative low enzyme content and short time. Comparison of predicted and experimental values showed good correspondence, implying that the empirical model derived from RSM can be used to adequately describe the relationship between the reaction parameters and the response (yield conversion) in lipase-catalyzed biodiesel synthesis. Copyright © 2008 Society of Chemical Industry [source] Characteristics of Immobilized Lipase on Hydrophobic Superparamagnetic Microspheres To Catalyze EsterificationBIOTECHNOLOGY PROGRESS, Issue 2 2004Zheng Guo A novel immobilized lipase (from Candida rugosa) on hydrophobic and superparamagnetic microspheres was prepared and used as a biocatalyst to catalyze esterification reactions in diverse solvents and reaction systems. The results showed that the immobilized lipase had over 2-fold higher activities in higher log P value solvents. An exponential increase of lipase activity against log P of two miscible solvent mixtures was observed for the first time. Both free and immobilized lipase achieved its maximum activity at the range of water activity ( aw) 0.5,0.8 or higher. At aw 0.6, the immobilized lipase exhibited markedly higher activities in heptane and a solvent-free system than did the native lipase. In multicompetitive reactions, the alcohol specificity of the lipase showed a strong chain-length dependency, and the immobilized enzyme exhibited more preference for a longer-chain alcohol, which is different from previous reports. The immobilized lipase showed higher specificities for butyric acid and the medium-chain-length fatty acids (C8,C12). Then, the immobilized lipase was extended to solvent-free synthesis of glycerides from glycerol and fatty acids. Recovered by magnetic separation, the immobilized lipase exhibited good reusability in repeated batch reaction, indicating its promising feature for biotechnology application. [source] Thermodynamic activity-based enzyme kinetics: Efficient tool for nonaqueous enzymologyAICHE JOURNAL, Issue 3 2001Georgina C. Sandoval Lipase-catalyzed synthesis reactions must be performed in nonaqueous media (organic solvents or solvent-free systems). The choice of the optimal solvent is usually a fastidious task that necessitates the determination of kinetic parameters in each solvent. The approach used here, to overcome the lack of a model that can predict the kinetics whatever the solvent, consists in the use of thermodynamic activities instead of concentrations of components, and assumes that activity-based kinetic parameters are the same in all solvents. This assumption is discussed, and a solution is proposed which takes into account some observed residual solvent effects. The reaction chosen to test this approach was the esterification of oleic acid with ethanol catalyzed by an immobilized lipase, Lipozyme. For this reaction, the kinetics predicted in various organic solvents and in solvent-free systems is in agreement with the experimental data. [source] | |||||||||||||