• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.2
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• pp.103-108
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• 1998

A hydrophobic substrate triolein was hydrolyzed by lipase in a mono-phase reaction system containing cyclodextrin(CD) as emulsifier. The triolein was transformation to an emulsion-like state in the CD containing reaction system in contrast to the oil-droplet like state without CD due to the formation of an inclusion complex between the lipids and CDs. The hydyrolysis reaction increased substantially in the CD containing reaction system, and the optimum reaction conditions including the amount of lipase, ${\beta}$-CD concentration, and mixing ratio of triolein and ${\beta}$-CD, were determined. The performance of the enzyme reaction in a mono-phase reaction system was compared with that of a two-phase reaction system which used water immiscible hexane as the organic solvent. The role of a CD in the mono-phase reaction system was elucidated by comparing the degree of the inclusion complex formation with triolein and oleic acid, Km and Vmax values, and product inhibition by oleic aicd in aqueous and CD containing reaction systems. The resulting enhanced reaction seems to be caused by two phenomena; the increased accessibility of lipase to triolein and reduced product inhibition by oleic acid through the formation of an inclusion complex.

• 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.

• Microbiology and Biotechnology Letters
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• v.19 no.4
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• pp.377-382
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• 1991

Reef tallow was hydrolyzed with lipase under the conditions of liquid state and solid state. Lipase OF 360 was used for that purpose, and the lipase had the maximum activity when the olive oil was used as a substrate at pH 6 and $37^{\circ}C$. Beef tallow was dispersed by an agitator to perform a liquid enzymatic reaction. Water content, reaction temperature, and enzyme amount were varied as parameters affecting hydrolysis percentage. Ninety three percents of tallow were hydrolyzed at the following conditions: water content 80% w/w, temperature $37^{\circ}C$, and enzyme amount 200 unitlg tallow. In order to conduct a solid phase enzymatic reaction, sonication was employed for pretreating tallow with the enzyme solution. Molten tallow was sonified with the enzyme solution, and solidified by lowering temperature. And then hydrolysis reaction proceeded at $30^{\circ}C$. Sonication intensity and time were varied to control hydrolysis percentage. Optimum values of the intensity and the time were found to exist since the hydrolysis percentage did not increase further according to the increases of the intensity and the time.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.3
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• pp.496-501
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• 1994

The synthesis of lauryl palmitate from palmitic acid and lauryl alcohol was investigated in organic solvents using lipase. Water-immiscible organic solvent such as hexane, toluenem cyclohexane, and isooctane were found to be suitable of ester synthesis . The effect of water content on the initial rate of conversion was examined . As the content increased, the reaction rate increased. But addition of water in organic solvent decreased therostability of enzyme . The best lauryl palmitate synthesis was achieved with water content of 0.2-0.4% reaction temperature of 4$0^{\circ}C$ and 45$^{\circ}C$ for Candida cylindracea lipase porcine, pancreatic lipase, respectively. when ester synthesis was carried out under the optimum conditions, the conversion yield of palmitate into lauryl palmitate after 70hrs reached 85% and 69 % for the Candida cylindracea lipase and porcine opancreatic lipase, respectivley.

• 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.

• Korean Journal of Agricultural Science
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• v.40 no.3
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• pp.227-235
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• 2013

This study was conducted to prove the effect of irradiation on lipases (lipase AK, lipase AH, lipase PS-D, Lipozyme TLIM, Lipozyme RMIM and Novozyme SP435) which were used for interesterification reaction using batch type reactor. Through such interesterification, structured lipid (1(3)-palmitoyl-2-oleoyl-3(1)-stearoyl, POS) was synthesized by lipase treated with irradiation at different doses (0, 3, 7, 14, 29 and 59 kGy) using canola oil, palmitic ethyl ester (PEE) and stearic ethyl ester (StEE). After the reaction, fatty acid composition of triacylglycerol (TAG) in structured lipid was analyzed to compare the lipase activity. The results showed that activity of the irradiated lipase AH, PS-D and Novozyme SP435 with certain dose (3 kGy) were slightly improved. Such change of lipase activity suggested that irradiation might affect on the interesterification properties. Especially, Lipase AK, Lipozyme TLIM and Lipozyme RMIM after at 3 kGy irradiation showed that content of stearic acid ($C_{18:0}$) was increased while palmitic acid ($C_{16:0}$) decreased in the interesterified products.

• Analytical Science and Technology
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• v.30 no.3
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• pp.138-145
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• 2017

Microwave-assisted organic synthesis has gained a remarkable interest over the past years because of its advantages - (i) rapid energy transfer and superheating, (ii) higher yield and rapid reaction, (iii) cleaner reactions. Ionic liquids are well known for their unique properties such as negligible vapor pressure and high thermal stability. With these properties, ionic liquids have gained increasing attention as green, multi-use reaction media. Recently, ionic liquids have been applied as reaction media for biocatalysis. Lipase-catalyzed reactions in ionic liquids provide high activity and yield compared to conventional organic solvents or solvent free system. Since polar molecules are generally good absorbent to microwave radiation, ionic liquids were investigated as reaction media to improve activity and productivity. In this study, therefore, the effect of microwave irradiation in ionic liquids was investigated on lipase catalyzed reactions such as benzyl acetate synthesis and caffeic acid phenethyl ester synthesis. Comparing to conventional heating, microwave heating showed almost the same final conversion but increased initial reaction rate (3.03 mM/min) compared to 2.11 mM/min in conventional heating at $50^{\circ}C$.

• Applied Biological Chemistry
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• v.39 no.1
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• pp.95-98
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• 1996

• Journal of Microbiology and Biotechnology
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• v.8 no.3
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• pp.191-196
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• 1998

This mini review describes the effects of water activity (${\alpha}_w$) on the kinetics, regio- and enantioselectivities of lipases, and various methods for measuring and controlling ${\alpha}_w$ in lipase catalyzed reaction in organic solvent.

• Microbiology and Biotechnology Letters
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• v.15 no.2
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• pp.122-128
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• 1987

Lipases from Candida rogosa and Rhizopus arrhizus were immobilized by entrapment with photo-crosslinkable resin prepolymer for the study of fat splitting and interesterification in isooctane-two phase system. Dioctylsulfosuccinate was selected as the most suitable surfactant during the immobilization. Lipase entrapped with hydrophobic photo-crosslinkable resin prepolymer(ENTP-3000) exhibited the highest activity, whereas lipase entrapped with hydrophilic gel(ENT-4000) was more stable in organic solvent. As the degree of hydrophobicity of the immobilization matrix was increased, Vm(app) of the lipase entrapped was increased, but Km(app) was approximately constant. While the optimum pH of the lipases entrapped on hydrophilic gel (ENT-4000) were around pH 7.0 for Candida lipase and Rhizopus lipase, the reaction rate of the lipases entrapped on hydrophobic gel were less dependent on pH variations for short reaction time. However, for longer reaction time, the lipnses from C. rugosa and R. arrhizus entrapped on hydrophobic gel yielded maximum rate at pH 6.0 and 6.5, respectively, Entrapment method endowed the lipase with thermal stability.