• KSBB Journal
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• v.14 no.6
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• pp.696-701
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• 1999

The enzymatic hydrolysis of Castor oil for the mass production of ricinoleic acid was studied to find out the optimum conditions such as solvents and the weight ratio of substrate to enzyme. Three different lipases were tested for the hydrolysis of castor oil: lipase from Porcine Pancrease(lipsase PP), lipase from Candida cylindracea(lipase CC), lipase from Candida Rugosa(lipase CR). The poor mass transfer in water caused a low degree of hydrolysis of castor oil. To overcome this problem, organic solvents were used. Among organic solvents tested, hydrophobic solvents gave better results of hydrolysis than hydrophilic solvents. Organic solvents also lowered or changed the effect of pH. Isopropyl ether made complete hydrolysis of castor oil. The ratio of water to isopropyl ether and the ratio of weight ratio of lipase to castor oil were important for the hydrolysis of castor oil. At 30$^{\circ}C$ castor oil was completely hydrolyzed by 4 wt% of lipase in the mixture of isopropyl ether and water(1:1 in volume).

• KSBB Journal
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• v.19 no.2
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• pp.148-153
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• 2004

Lipase catalyzes the hydrolysis of glycerides into fatty acids and glycerol. The study of microbial lipases has been stimulated in resent years. It is due to the potential uses of lipases in esterification of oils to glycerol, alcohols and carbohydrates. Development of lipase producing yeast has been focused concerning to the utilization of yeast culture for animal feed. In this study, yeast like cells was isolated from a waste oil and sludge. A strain having higher lipase activity was selected by random mutagenesis using UV-radiation. The optimal cultivation conditions in submerged culture were examined in terms of lipase production. 2.0％ of high fructose syrup, 1,0％ of CSL, and 1.0％ of olive oil were selected as the nutritional media for the production of lipase. The maximum lipase activity of 1.12 U/ml and viable cell number of 8.8${\times}$10$\^$7/ cells/mL were obtained at 27$^{\circ}C$ with an initial pH of 5.0.

• Journal of Korean Medicine for Obesity Research
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• v.17 no.2
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• pp.101-110
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• 2017

Objectives: In this study, the lipolytic effects of Eriobotrya folium extract (EFE) on local fat was investigated in high fat diet (HFD)-induced obesity mouse and 3T3-L1 adipocytes. Methods: C57BL/6J mice (5 weeks) were fed HFD for 6 weeks to induce obesity. EFE (20 mg/ml, $100{\mu}l$) or saline ($100{\mu}l$) as a normal control was injected into left inguinal fat pad region, 3 times per a week for last 2 weeks. After sacrifice, body weight, and histological changes of the inguinal fat pad were evaluated. The expressions of hormone-sensitive lipase (HSL) and adipose triglyceride lipase (ATGL) in inguinal fat pad were analyzed by Western blotting. Also, lipid accumulation and lipases release were determined in 3T3-L1 adipocytes by oil red o staining. Results: EFE significantly reduced the weight of inguinal fat pad and the size of adipocytes in HFD-induced obesity mice compared to control. The treatment of EFE up-regulated the expressions of HSL and ATGL in inguinal fat pads of obesity mice, as well as 3T3-L1 adipocytes. In addition, EFE inhibited the lipid accumulation in 3T3-L1 adipocytes in a dose dependent manner. Conclusions: EFE showed lipolytic effect on local fat of HFD-induced obesity mice by up-regulation of the lipases secretion. This suggests that EFE could be considered as anti-obese substance with lipolytic property on local fat.

• Microbiology and Biotechnology Letters
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• v.15 no.2
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• pp.98-103
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• 1987

Two phase reaction system was used to hydrolyze the olive oil for fat splitting. Kinetics of lipases in two phase system were investigated by determining the hydrolysis rate of triglycerides at various olive oil concentrations in isooctane using the microbial lipases from Candida rugosa and Rhizopus arrhizus. The rate equation in lipid hydrolysis for various olive oil concentrations in two phase system was deviated from the Michaelis-Menten kinetics. The results suggested that the olive oil concentration in isooctane affects the interfacial area. The dependency of the interfacial area on olive oil concentration is greater at the lower olive oil concentration than at the higher substrate concentration. We modified the rate equation by considering the interfacial area between two phases depending on the olive oil concentration in solvent phase.

• Journal of Life Science
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• v.29 no.4
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• pp.492-498
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• 2019

Previously, three kinds of lipases, lipAD1, lipAD2, and lipAD3, and lipase chaperone, lipBD, of Acinetobacter schindleri DYL129 isolated from soil sample were reported. In this report, three lipase and lipase chaperone were cloned into the pET32a(+) or pGEX-6P-1 vectors for protein expression in Escherichia coli, and named as pETLAD1, pETLAD2, pETLAD3 and pETLBD or pGEXLAD1, pGEXLAD 2, pGEXLAD3 and pGEXLBD, respectively. Protein expression rate was higher in pET system than in pGEX system. Although LipAD1 and LipAD2 were produced as inclusion bodies, their expression levels were high. So LipAD1 and LipAD2 could be solubilized in 8 M urea buffer and purified. LipAD3 and LipBD were overexpressed in soluble form and purified. Those proteins were purified by His-tag affinity chromatography connected in AKTA prime system. The activities of the purified lipases were demonstrated with 1% tributyrin agar plate. After purification, molecular mass was determined with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. LipAD1 showed high activity toward ${\rho}$-nitrophenyl acetate and ${\rho}$-nitrophenyl butyrate, LipAD2 showed high activity toward ${\rho}$-nitrophenyl acetate and ${\rho}$-nitrophenyl myristate, and LipAD3 showed high activity toward ${\rho}$-nitrophenyl acetate, ${\rho}$-nitrophenyl butyrate, and ${\rho}$-nitrophenyl miristate, respectively. Three lipases, LipAD1, LipAD2, and LipAD3, showed optimal reaction at $50^{\circ}C$ using ${\rho}$-nitrophenyl butyrate, as substrate.

• Journal of Microbiology and Biotechnology
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• v.27 no.4
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• pp.649-659
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• 2017

Extremophilic microorganisms have established a diversity of molecular strategies in order to survive in extreme conditions. Biocatalysts isolated by these organisms are termed extremozymes, and possess extraordinary properties of salt allowance, thermostability, and cold adaptivity. Extremozymes are very resistant to extreme conditions owing to their great solidity, and they pose new opportunities for biocatalysis and biotransformations, as well as for the development of the economy and new line of research, through their application. Thermophilic proteins, piezophilic proteins, acidophilic proteins, and halophilic proteins have been studied during the last few years. Amylases, proteases, lipases, pullulanases, cellulases, chitinases, xylanases, pectinases, isomerases, esterases, and dehydrogenases have great potential application for biotechnology, such as in agricultural, chemical, biomedical, and biotechnological processes. The study of extremozymes and their main applications have emerged during recent years.

• Journal of Microbiology and Biotechnology
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• v.4 no.2
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• pp.85-94
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• 1994

Lipase (triacylglycerol hydrolase, EC 3.1.1.3) is able to catalyze the hydrolysis of ester bonds of triacylglycerols at the interface between aqueous phase and organic phase containing substrate. With the rapid development of lipid biotechnology, lipase-catalyzed hydrolysis of lipids has a great concern from the industrial point of view. Owing to the reversible nature of the lipase, the reactions are also applied for glyceride synthesis, interesterification and resolution of racemic mixtures into optically active alcohols or acids. For all applications of the lipases, a reliable method for the determination of enzyme activity is required. Precise quantitative determination of its activity is essential as the basis of research and development of the bioprocess involving the enzyme. This article reviews the existing literature on the detection and determination of lipase activity from microbial, mammalian and plant sources.

• BMB Reports
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• v.34 no.3
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• pp.274-277
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• 2001

Lipase of Staphylococcus sp. was purified from the culture supernatant, and its molecular mass estimated to be 44 kDa by SDS-PAGE. Its optimum temperature and pH for the hydrolysis of p-nitrophenyl substrates was $28^{\circ}C$ and pH 8.5, respectively The gene encoding the lipase was cloned in Escherichia coli in the $NH_2$-teminally truncated form by using the shotgun method, and sequenced. The mature enzyme had a 49-93% amino acid sequence homology with other staphylococcal lipases. This lipase was used for the hydrolysis of the 3-O-acetate of cephalosporin-C to give an intermediate, deacetylated cephalosporin-C that is useful for further chemical elaborations.

• Journal of the Korean Applied Science and Technology
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• v.20 no.3
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• pp.251-258
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• 2003

Biodiesel as methyl esters derived from vegetable oils has considerable advantages in terms of environmental protetion. In the present work, methyl esters were produced from soybean oil by lipase-catalyzed transesterification. To reduce inactivation of commercial immobilized lipases emulsified two-step process was developed using the stepwise addition of methanol with 4:1 molar ratio at 4h intervals. Also with immobilized lipase from Candida antarctica(Novozym 435) high conversion of 98.5 percent was possible at $45^{\circ}C$ of reaction temperature with 4:1 of methanol-to-oil molar ratio and 1%(v/v) methyl glucoside oleic polyester as an emulsifier in the presence of cosolvent.

• Fisheries and Aquatic Sciences
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• v.12 no.1
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• pp.16-23
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• 2009

Lipids were extracted from marine rotifer, Brachionus rotundiformis in order to examine the functionality of lipid enzymatic modification. The fatty acids, palmitic, linoleic, oleic and stearic acids were the dominant forms accounting for approximately 35.8%, 21.5%, 15.9% and 7.7% of the total lipid content, respectively. Lipid fractions were categorized as neutral lipids (38.5%), glycolipids (45.9%) and phospholipids (17.6%), and after extraction from the rotifer were isolated by thin-layer chromatography (TLC) as free fatty acids (FFA), monoacylglycerol (MAG), diacylglycerol (DAG) and triacylglycerol (TAG). The production of polyunsaturated fatty acid (PUFA) concentrate from rotifer lipids was studied using lipase-catalyzed hydrolysis. In addition, rotifer lipids were modified by hydrolysis using lipases such as porcine pancreas, Candida rugosa and Rhizomucor miehei. The lipase from Rhizomucor miehei was effective in extracting linoleic acid (C 18:2), while the lipase from Candida rugosa was effective in palmitic acid (C16:0) extraction.