• Journal of Microbiology and Biotechnology
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• v.8 no.2
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• pp.165-170
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• 1998

Lipase-catalyzed esterification of n-butyl oleate was carried out in n-hexane as a model reaction. The optimal activity of Candida rugosa lipase was shown in a water activity ($a_w$) range of 0.52 to 0.65 at $30^{\circ}C$. The water produced from the esterification was removed by a tubular type pervaporation system. The rate of ester formed from the enzymatic esterification was allowed to be the same as the rate of water removal by maintaining an optimal $a_w$ of the reaction system using an on-off dewatering control device. The reaction rate and yield with a$a_w$ control were increased two folds higher than the respective values for the uncontrolled reaction.

• KSBB Journal
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• v.17 no.6
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• pp.543-548
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• 2002

The enantioselective esterification of racemic ibuprofen catalyzed by a Candida rugosa lipase was studied according to reaction conditions such as a lipase concentration, reaction temperature, alcohol chain length and alcohol concentration. The S-(+)-ibuprofen alkyl esters prepared were converted to S-(+)-ibuprofen by hydrolysis with sulfuric acid as a catalyst. High conversions in the esterifications were obtained at 60$^{\circ}C$ and an equimolar ratio of octanol to ibuprofen. The initial reaction rate of the esterification decreased with increasing octanol concentration. Conversion and initial reaction rate increased with increasing alcohol chain length. Values of enantiomeric excess(ee) according to esterification reaction conditions did not change below 60$^{\circ}C$. On the other hand, values of conversion and ee for the chemical hydrolysis of S-(+)-ibuprofen alkyl esters were independent of alcohol alkyl chain length. Optical resolution of racemic ibuprofen was achieved by lipase catalyzed esterification and chemical hydrolysis. The separation method provided a high yield and enantioselectivity for the production of S-(+)-ibuprofen from racemic ibuprofen.

• Journal of the Korean Applied Science and Technology
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• v.22 no.2
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• pp.106-115
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• 2005

Bio-diesel as fatty acid methyl ester was derived from such oils as soybean, peanut and canola oil by lipase catalyzed continuous trans-esterification. So the activation of lipase(Novozym - 435) was kept to be up to 4:1, the limiting molar ratio of methanol to oil under one-step addition of methanol due to the miscibility of oil and methanol through the static mixer for 4hrs and the elimination of glycerol on the surface of lipase by 7wt% silica gel. Therefore the overall yield of fatty acid methyl ester from soybean oil appeared to be 98% at 50$^{\cdot}C$ of reaction temperature under two-steps addition of methanol with 2${\times}$2:1 of methanol to oil molar ratio at an interval of 5.5hrs, 7wt% of lipase, 24 number of mixer elements, 0.2ml/min of flow rate and 7wt% of silica gel.

• Journal of Microbiology and Biotechnology
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• v.19 no.12
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• pp.1596-1602
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• 2009

A lipase-catalyzed esterification reaction of (S)-naproxen ethyl ester by CALB (Candida antarctica lipase B) enzyme was performed in supercritical carbon dioxide. Experiments were performed in a high-pressure cell for 10 h at a stirring rate of 150 rpm over a temperature range of 313.15 to 333.15 K and a pressure range of 50 to 175 bar. The productivity of (S)-naproxen ethyl ester was compared with the result in ambient condition. The total reaction time and conversion yields of the catalyzed reaction in supercritical carbon dioxide were compared with those at ambient temperature and pressure. The experimental results show that the conversion and reaction rate were significantly improved at critical condition. The maximum conversion yield was 9.9% (216 h) at ambient condition and 68.9% (3 h) in supercritical state. The effects of varying amounts of enzyme and water were also examined and the optimum condition was found (7 g of enzyme and 2% water content).

• Journal of the Korean Applied Science and Technology
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• v.21 no.1
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• pp.37-44
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• 2004

Glycosyl acrylate and methacrylate were synthesized by lipase-catalyzed esterification of vinyl acrylate and vinyl methacrylate with ${\beta}$-methyl glucoside in t-butanol as a reaction medium. At the optimum conditions of initial concentration of 150g/l ${\beta}$-methyl glucoside, molar ratio of 1 : 3, 5%(w/v) lipase(Novozym 435) and $50^{\circ}C$, we attained up to 100% conversion for enzymatic glycosylation of vinyl acrylate and vinyl methacrylate by supersaturated solvent process. The polymerizable glycosyl acrylates and methacrylate are expected to have biomedical application as hydrophilic monomers and hydration modifiers to be used for biocdmpatible hydrogel.

• Biotechnology and Bioprocess Engineering:BBE
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• v.7 no.2
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• pp.76-84
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• 2002

On-line conversion estimation of enzymatic esterification reactions in solvent-free media was investigated. In principle, conversion to ester can be determined from the amount of water produced by the reaction, because water is formed as a by-product in a stoichiometric manner. In this study, we estimated the water production rate only from some measurements of relative humidity and water balances without using any analytical methods. In order to test the performance of the on-line conversion estimation, the lipase-catalyzed esterification of n-capric acid and n-decal alcohol in solvent-free media was performed whilst controlling water activity at various values. The reaction conversions estimated on-line were similar to those determined by offline gas chromatographic analysis. However, when the water activity was controlled at higher values, discrepancies between the estimated conversion values and the measured values became significant. The deviation was found to be due to the inaccurate measurement of the water content in the reaction medium during the initial stages of the reaction. Using a digital filter, we were able to improve the accuracy of the on-line conversion estimation method considerably. Despite the simplicity of this method, the on-line estimated conversions were in good agreement with the off-line measured values.

• Journal of Microbiology and Biotechnology
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• v.11 no.6
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• pp.951-956
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• 2001

A 28-kDa extracellular lipase (pI 8.7) was purified to homogeneity from the culture supernatant of Trichosporon sp. Y- 11 by mmonium sulfate precipitation, DEAE-Sephadex A-50, Bio-Gel P-30, CM- Sephadex C-50, and Bio-Gel P- 10 chromatographies. The purified enzyme exhibited a specific activity of $2,741{\;}{\mu}mol/min/mg$ based on the hydrolysis of triolein, and the optimal hydrolysis activity was dentified at pH 8.0 and $40^{\circ}C$. The enzyme activity was inhibited by $Ag^+$ and enhanced by $Fe^{2+}$, $Fe^{3+}$, $Mg^{2+}$, $Mn^{2+}$, and $Li^{+}$. The enzyme activity exhibited for the hydrolysis of both tributyrin and trilinolein. The ester synthesis of unsaturated fatty acids with various alcohols catalyzed by the purified lipase in a nonaqueous medium or microaqueous system was also investigated. The esterification activity of the lipase increased with an increase of the carbon chain length in the alcohol. The synthesis rate of linoleic acid and oleyl alcohol was the highest with an optimal temperature and pH of $40^{\circ}C$ and 8.0, respectively. The water content and agitation also affected the esterification activity of the lipase.

• Applied Chemistry for Engineering
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• v.18 no.6
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• pp.643-649
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• 2007

Lipase-catalyzed esterification of structural butanol isomers and n-butyric acid was investigated in supercritical carbon dioxide. The experiments were performed in a high pressure cell for 5 hrs with a stirring rate of 150 rpm at 323.15 K and 130 bar. The Candida Antarctica lipase B (CALB) was used in whole system as a catalyst. The experimental results were analyzed by GC-FID using a INNOWax capillary column. The conversion yield and the tendency of the esterification in supercritical carbon dioxide were compared with estimated results by molecular dynamics simulation. Based on the Ping-Pong Bi-Bi mechanism with competitive inhibition, each step of the reaction was optimized; using this result the transition state was predicted. Conformational preference of isomers was also analyzed using molecular dynamics simulations. This kind of approach will be further extended to the prediction of enzyme-catalyzed reactions using computers.

• Proceedings of the Membrane Society of Korea Conference
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• 2004.05a
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• pp.187-190
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• 2004

Microemulsions gelled by the aid of natural polymers, i.e. microemulsion-based organogels (MBGs), have become of interest as novel tools for enzyme immobilization in hydrophobic solvents [1,2]. Sodium bis(2-ethylhexyl) sulfosuccinate (AOT)is frequently employed as an amphiphile for stable MBG formation.(omitted)

• Korean Journal of Food Science and Technology
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• v.35 no.5
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• pp.797-802
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• 2003

Structured lipids (SL) were synthesized by esterification of corn oil and conjugated linoleic acid (CLA) in a continuous packed-bed column reactor. The effects of flow rate, reaction temperature, and substrate molar ratios were studied. The reaction was catalyzed by TL IM (immobilized lipase from Thermomyces lanuginosa). Results of triacylglycerol (TAG) analysis by GC showed that the incorporated CLA isomers were mainly cis9, trans11- and trans 10, cis12-CLA. Slower flow rates yielded higher incorporation, and maximum incorporation of CLA was obtained with a molar ratio of 1:3 (corn oil: CLA) at a temperature of $55^{\circ}C$. The obtained SLs had iodine values ranging from 120 to 128. The SLs were composed of TAG $(98{\sim}99%)$, 1,2- and 1,3-diacylglycerol ($0.7{\sim}1.3%$), and a small amount of monoacylglycerol.