• Korean Chemical Engineering Research
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• v.48 no.1
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• pp.121-127
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• 2010

This study is to optimize the enzyme(lipase) activity for biodiesel production. The ion-exchanged non-woven fabrics(EtA, DEA-EtA non-woven fabric) containing ethanolamine, diethylamine groups are used by radiation induced grafted polymerization onto a non-woven fabric for more effective immobilization of lipase. Since the porous hollow fiber membranes are showed the low throughputibehe non-woven fabric membranes are used for biodiesel production. The physical charateristics of enzyme immobilized and the enzyme activity to EtA and DEA-EtA non-woven fabrics are studied. The EtA non-woven fabrics are quite similar to DEA-EtA non-woven fabric for the amount of enzyme immobilized(EtA non-woven fabric:15.69 mg/g, DEA-EtA non-woven fabric:14.45 mg/g) but DEA-EtA non-woven fabrics have shown the lower permeabiliquite the organic solvent than the EtA non-woven fabrics(EtA non-woven fabric:$3.50mol/h{\cdot}kg$, DEA-EtA non-woven fabric:$0.38mol/h{\cdot}kg$). Optimum characteristics of ehe non-woven fabric membranes and the limilaractivity are also investigated for the effective biodiesel production.

• BMB Reports
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• v.30 no.1
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• pp.7-12
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• 1997

The kinetics of the interesterification of triolein and stearic acid catalyzed by immobilized Rhizopus delemar lipase were studied in a batch operation. In order to clarify the mechanisms of this reaction, three models are discussed under various conditions in terms of the ratio of triolein and stearic acid. The rate constants involved in the proposed model were determined by combining the numerical Gauss-elemination method, and the trial-and-error method so as to fit the calculated results with the experimental data. The accuracy of the obtained rate constants was confirmed after they were substituted for simultaneous differential equations and the equations simulated using an adaptive step-size Runge-Kutta method. Finally, the model which agrees with the calculated results and the experimental data was selected.

• Proceedings of the Korean Society of Postharvest Science and Technology of Agricultural Products Conference
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• 2003.10a
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• pp.164.2-165
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• 2003

Structured lipids (SLs) are defined as triacylglycerols to change the fatty acid composition in the glycerol backbone and lipases are known as a powerful tool for the syntheses of SLs. Structured lipid from corn oil, capric acid, and conjugated linoleic acid (CLA) by transesterification reaction and using several amounts of immobilized lipase RM IM (from Rhizomucor miehei) was studied, and 4% of lipase amount was selected for further study as the optimal amount. Comparison the chemical properties (free fatty acid value, iodine value, saponification value, tocopherols, and color analysis), solidification behavior, and volatile fractions (from headspace SPME GC-MS) between com oil and SL com oil was obtained.

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.229-229
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• 2003

• Journal of Marine Bioscience and Biotechnology
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• v.1 no.4
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• pp.311-316
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• 2006

Enzymatic ethanolysis of fish oil with immobilized lipase was investigated for reducing the free fatty acid contents and enhancing the function of fish oil. Ethanolysis reactions were carried out in erlenmeyer flask (25ml) containing a mixture of squid viscera oil and 99.9% ethanol using 1% (based on w/w squid viscera oil) immobilized lipase. The reaction mixtures were incubated at $50^{\circ}C$ and shaken at 100rpm. Ethanol was added into the mixture by stepwise addition method of Shinmada[9]. Measurement of free fatty acid molar amounts was studied by Acid Value. Tendency of oil variation during transesterification was studied by TLC method. Enzymatic ethanolysis composed diglyceride, monoglyceride and fatty acid ethyl ester with reducing free fatty acid contents. Also, selective ethanolysis by Lipozyme TL-IM and Lipozyme RM-IM mostly did not react at the sn-2 position of squid viscera oil. Lipozyme RM-IM was more suitable enzyme to reduce the free fatty acid contents by ethanolysis than Lipozyme TL-IM. Squid viscera oil was transformed into suitable properties (5 in Acid Value) for functional fish oil production.

• Applied Chemistry for Engineering
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• v.16 no.6
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• pp.731-736
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• 2005

In this paper, immobilization of lipase (Rhizomucor miehei, Rhm) onto ion-exchange resin pretreated with oleic acid and its application were studied. Immobilization efficiency was reached to 82% when weakly basic anion exchange resin, Duolite A-568, was used. Immobilized Rhm was stable in water, chloroform and hexane, however, unstable in alcoholic solvents. When immobilized Rhm was applied to the esterification reaction of glycerol and fatty acid, content of DG in the product mixture was ca. 80 mol% and 1,3-DG in total DG reached to 98%.

• Microbiology and Biotechnology Letters
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• v.37 no.4
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• pp.365-370
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• 2009

For the production of diglyceride (DG) containing medium chain fatty acid, which could be utilized as a substrate to structured lipid production, monoglyceride (MG) and caprylic acid were reacted in the presence of lipase. The reaction system was well mixed homogeneously without using any organic solvent. Among the lipases investigated, Lipozyme RM IM and Novozym 435 were selected on the basis of equilibrium DG yields from the medium chain fatty acid and MG. And reaction conditions such as addition of molecular sieve, water content of immobilized lipase, reaction temperature, and mole ratio of MG/caprylic acid are optimized to increase DG production by using Lipozyme RM IM. DG content of reaction mixture showed 8% increase by adding molecular sieve to reaction mixture. Removal of water from the immobilized lipase could affect seriously equilibrium content of DG. More than 2.8%(w/w) removal of water from the support could make 44% of DG. Optimum temperature was found to $60^{\circ}C$. Temperature shift from $60^{\circ}C$ to $25^{\circ}C$ resulted in increase of free fatty acid (FFA) content. The equilibrium DG yield was not seriously affected by on MG/caprylic acid molar ratio. However, at the stoichiometric ratio of 1:1 the highest DG yield was obtained. Increasing MG/caprylic acid ratio from 0.3 to 1.8 decreased FFA content from 34% to 13%, while MG content increased from 27% to 50%.

• Applied Biological Chemistry
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• v.51 no.3
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• pp.177-182
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• 2008

This study was carried out to investigate the reaction of lipase-catalyst transesterification using animal fat recovered from fleshing scrap generated during leather making process. Transesterification reaction between fat and primary or secondary alcohol was carried out under the condition of immobilized enzyme catalyst. The conversion rate was the highest when 1.5 mole of methanol was injected by 4 times. As for lipase, Candida antarctica showed the highest conversion rate of 82.2% among the 4 different lipases. It was found that water contained in the fat causes lower conversion rate. The condition of 1.2wt. % of water in the fat decreased the conversion rate by 40%. It was considered that the resulted reactant, fatty acid ester could be used as raw material for biodiesel with the characteristics of not generating SOx and diminishing smoke.

• Journal of Life Science
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• v.26 no.5
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• pp.603-607
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• 2016

A crude extracellular lipase from solvent-tolerant bacterium Pseudomonas sp. BCNU 106 was highly stable in the broad pH range of 4-10 and at temperature of 37℃. Crude lipase of BCNU 106 exhibited enhanced stability in 25% organic solvents such as xylene (121.85%), hexane (120.35%), octane (120.41 %), toluene (118.14%), chloroform (103.66%) and dodecane (102.94%) and showed excellent stability comparable with the commercial immobilized enzyme. In addition, the stability of BCNU 106 lipase retained above 110% of its enzyme activity in the presence of Cu²⁺, Hg²⁺, Zn²⁺ and Mn²⁺, whereas Fe²⁺ strongly inhibited its stability. The detergents including tween 80, triton X-100 and SDS were positive signals for lipase stability. Because of its stability in multiple organic solvents, cations and surfactants, the Pseudomonas sp. BCNU 106 lipase could be considered as a potential biocatalyst in the industrial chemical processes without using immobilization.

• Journal of Life Science
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• v.23 no.10
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• pp.1246-1251
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• 2013

An organic solvent-tolerant lipase of Pseudomonas sp. BCNU 154 that was isolated from wastewater in the industrial complex region had optimal activity at $37^{\circ}C$ and pH 8. This crude extracellular lipase from BCNU 154 exhibited maximum stability in toluene, retaining about 6.01 U/ml (117.53%) activity for 2 h. $Ca^{2+}$, $Mg^{2+}$, $NH_4{^+}$, and $Na^+$ ions and triton X-100 activated the enzymes, whereas $Ba^{2+}$, $Hg^{2+}$, and $Zn^{2+}$ ions inhibited their activity. Pseudomonas sp. BCNU 154 lipase revealed stable activity comparable to that of the commercial immobilized Novozym 435. Thus, this organic solvent-tolerant lipase could have potential as a whole cell biocatalyst in industrial chemical processes without the use of immobilization.