• 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.6 no.4
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• pp.337-344
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• 1991

The liquid-liquid extraction of lipase A from Candide cylindracea and lipase B from porcine pancrease was carried out using reversed micellar organic solvents. Effects of various factors such as ionic strength, pH, and species and concentration of surfactant, on lipase solubilization were studied. A cationic surfactant cetyl-trimethyl ammonium bromide (CTAB) in isooctane/nhexanol(1:1) was found to be an effective solvent and its optimum concentration was 50 mM. KCl among various salts tested was the most effective and the efficiency of solubilization of lipase increased with decreasing the ionic strength of salts. The maximum activity and solubiliz ation of protein were obtained at pH 8. The stripping efficiency has a maximum value at pH 4 and increases with KCl concentration in the range of 0.2∼1.0 M. After the solubilization and stripping, the overall recovery efficiency of mass and specific activity of lipases was 62% and 66%, respectively.

• Proceedings of the Membrane Society of Korea Conference
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• 2003.07a
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• pp.65-68
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• 2003

The paper discusses the use of stable emulsion, prepared by membrane emulsification technology, to improve the enantiocatalytic performance of immobilised lipase in multiphasic membrane reactors. The production of optical pure (S)-naproxen from racemic naproxen methyl ester has been used as model reaction system. The enzyme was immobilised in the sponge layer (shell side) of capillary polyamide membrane with 50 kDa cut-off, The O/W emulsion, containing the substrate in the organic dispersed phase, was fed to the enzyme membrane reactor from shell-to-lumen. The results evidenced that lipase maintained stable activity during all the operation time (more than 250 hours), showing an enantiomeric excess (96 $\pm$2%) comparable to the free enzyme (98 $\pm$ 1%) and much higher compared to similar lipase-loaded membrane reactors used in two-separate phase systems (90%). The study showed that immobilised enzymes can achieve high stability as well as high catalytic activity and enantioselectivity.

• Journal of Life Science
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• v.25 no.3
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• pp.299-306
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• 2015

Chrysanthemum zawadskii, a herbaceous perennial plant belonging to the Compositae, grows wild in Asian countries, including Japan, China, and Korea. The biological, antioxidative, anti-inflammatory, and antibacterial activities of C. zawadskii have been reported, its antiobesity activity has not been elucidated. In the present study, the effect of C. zawadskii methanol extract (CZME) on pancreatic lipase enzyme activity, adipocyte differentiation, and adipogenesis was investigated using an in vitro assay and a cell model system. CZME effectively suppressed lipase enzyme activity in a dose-dependent manner. CZME also inhibited insulin, dexamethasone, 3-isobutyl-1-methylxanthine (MDI)-induced adipocyte differentiation, lipid accumulation, and the level of triglyceride in 3T3-L1 preadipocytes in a dose-dependent manner, without cytotoxicity. The antiobesity effect of CZME might be modulated by gene and protein expression of cytidine-cytidine-adenosine-adenosine-thymidine (CCAAT)/enhancer binding proteins (C/EBP) α, C/EBPβ, and the peroxisome proliferator-activated receptor γ (PPAR γ). CZME also triggered lipolysis in a dose-dependent manner in MDI-induced 3T3-L1 preadipocytes. Taken together, these results provide important new insights into the antiobesity activities of C. zawadskii, showing that they involve pancreatic lipase inhibition, as well as antiadipogenic and lipolysis effects. CZME might be a promising source in the field of nutraceuticals. However, the active compounds that confer the antiobesity activities of CZME need to be identified.

• Microbiology and Biotechnology Letters
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• v.42 no.3
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• pp.249-257
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• 2014

In this study, the anti-oxidative and anti-obesity activities of Amomum cardamomum L. methanol extract (ACME) were evaluated using DPPH radical scavenging activity assay, pancreatic lipase enzyme inhibition assay, and the cell culture model system. ACME exhibited DPPH radical scavenging activities dose-dependently, with $IC_{50}$ of DPPH radical scavenging activities of ACME being $25.15{\mu}g/ml$. Furthermore, ACME effectively suppressed pancreatic lipase enzyme activity dose-dependently. ACME also significantly suppressed adipocyte differentiation, lipid accumulation, triglyceride (TG) contents, and triggered lipolysis activity on 3T3-L1 preadipocytes in a dose-dependent manner, without cytotoxicity. Their anti-obesity effect was modulated by the cytidine-cytidine-adenosine-adenosine-thymidine (CCAAT)/enhancer binding proteins ${\alpha}$ ($C/EBP{\alpha}$), $C/EBP{\beta}$ and the peroxisome proliferator-activated receptor ${\gamma}$ ($PPAR{\gamma}$) gene and protein expressions. Taken together, these results provide an important new insight that A. cardamomum L. possesses anti-oxidative and anti-obesity activities such as pancreatic lipase inhibition, anti-adipogenic, and lipolysis effects. There is therefore potential for its use as a promising component in the field of nutraceuticals and the identification of the active compounds that confer the anti-oxidative and anti-obesity activities of ACME might be an appropriate next step.

• Journal of the Korean Society of Food Science and Nutrition
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• v.43 no.7
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• pp.1025-1035
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• 2014

This study assessed the effect of immobilized lipase on weak base styrene resin using polyethyleneimine (PEI) with cross-linking. Two procedures were used in this study. The first one, "mono-layer" lipase immobilization, involves washing PEI after adsorption. The second procedure, "multi-layer" lipase immobilization, has no washing before the cross-linking step. Treverlite XS-100200 (weak base styrene resin) was immersed with PEI solution (2.2 mg/mL). Lipase AH (from Burkholderia cepacia) was adsorbed onto the support coated with PEI before cross-linking with glutaraldehyde. Structured lipid was synthesized by immobilized lipase-catalyzed interesterification using canola oil, palmitic ethyl ester (PEE), and stearic ethyl ester (StEE). Total fatty acid contents of triacylglycerol (TAG) in structured lipids were analyzed to investigate activity, properties, and reusability of immobilized lipases. Activities of immobilized lipases on the multi-layer and mono-layer increased at a high concentration (8 mg/mL) of lipase solution used for immobilization. The results show that immobilized lipase with the mono-layer method at pH 8.0 on resin had the highest total saturated fatty acid content (26.17 area%). Activity of immobilized lipase with the multi-layer method at pH 7.5 on support was lower than that of the mono-layer, but total saturated fatty acid content was 16.79 area% higher than that of lipase AH (15.01 area%).

• Korean Journal of Fisheries and Aquatic Sciences
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• v.23 no.2
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• pp.69-76
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• 1990

To substitute the soy-sauce 'koji' used in fish sauce processing with molded sardine meal(MSM) 'koji', the culture conditions of MSM be inoculated with Aspergillus spp. were investigated. To prepare the MSM, Asp. awamori(KFCC. 11439), Asp. guercinus (KFCC. l1595), Asp. niger(KFCC. 11239), Asp. oryzae(KFCC. 32343), and Asp. sojae(KFCC. 11559) were inoculated upon the chopped sardine with $20\%$ (w/w) corn starch after steriling it at $121^{\circ}C$ for 15min. Sporulation time cultured with Asp. spp. at $30^{\circ}C$ was 48hrs and color of mycelium on the surface of MSM inoculated with Asp. awamari and Asp. oryzae were black, that of MSM inoculated with the other strains were yellowish brown. The activity of protease and lipase from the MSM were increased till the 72hrs of culture at $30^{\circ}C$, while the content of trimethylamine was decreased after 96hrs of culture period at same condition with exception of Asp. niger. Asp. oryzae and Asp. sojae showed superior in pro-tease and lipase activity in comparison with the other strains, and maximum activity of protease and lipase of MSM was observed after 72hrs of culture period. The optimum pH and temperature for the activity of MSM inoculated with Asp. oryzae and Asp. sojae were pH 9.0, $30\~35^{\circ}C$ and pH $6\~7$, $35^{\circ}C$, respectively.

• Food Science and Preservation
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• v.18 no.1
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• pp.53-58
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• 2011

Activity-guided isolation from an ethylacetate-soluble fraction of a 70% (v/v) ethanolic extract from the roots of Taraxacum ohwianum, using a pancreatic lipase inhibition assay, resulted in isolation and identification of five phenolic metabolites of previously known structure; these were 3,5-di-O-caffeoylquinic acid, chicoric acid, caffeic acid, protocatechuic aldehyde, and luteolin. All structures were confirmed by NMR and MS scpectroscopic data. Of these compounds 3,5-di-O-caffeoylquinic acid exhibited the most potent inhibitory activity, with $IC_{50}$ of $65.1{\pm}0.7\;{\mu}M$ against pancreatic lipase.

• The Korean Journal of Food And Nutrition
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• v.24 no.2
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• pp.153-158
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• 2011

This study was performed to develop new anti-obesity agents from medicinal plants for functional food industry. We prepared lipase inhibitor-containing ethanol extracts from Desmodium oxyphyllu DC. and its nutritional characteristics, stability of temperature and pH and physiological functionalities were investigated. Crude lipid content and curde protein content of ethanol extract from Desmodium oxyphyllum DC. were 26.5% and 5.7%, respectively and its asparagine content was 4,860 mg/100 g, dry basis. The ethanol extracts were also stable from pH 3.0 to pH 9.0 and below $80^{\circ}C$. The ethanol extract were showed high lipase inhibitory activity of 74.2% and acetylcholinesterase inhibitory activity of 68.4%.

• Journal of the Korean Society of Clothing and Textiles
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• v.33 no.7
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• pp.1121-1127
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• 2009

This study presents an eco-friendly and one-step finishing method for modifying fiber property that reduces fiber damage in wool/polyester blend fabrics. Lipase from aspergillus oryzae is used in this experiment. The enzymatic treatment condition is optimized by measuring the relative activity of lipase depending on pH level, temperature, concentration of lipase, and treatment time. The concentration of $CaCl_2$as an activator is determined by the characteristics including whiteness, water contact angle (WCA), and dyeing property. The modified properties of lipase treated fabrics are tested for pill resistance and surface morphology. The results are described as follows: the optimum condions for lipase treatment constitute a pH level of 8.0, treatment temperature of 40$^{\circ}$$_C$, concentration of lipase at 100% (o.w.f), and a treatment time of 90 minutes. $CaCl_2$helps in raising lipase activation, and the optimum concentration is 50mM. The whiteness, wet ability, and pill resistance of lipase treated fabrics improves as compared to the control. The dyeing property of lipase treated fabrics improved by 53.5% after using the one-bath dyeing method. This means that lipase treatment can save time and cost during the dyeing process since lipase treatment modifies wool and polyester fibers. The surface of lipase treated wool fibers do not exhibit any change, however voids and cracks manifest on the surface of lipase treated polyester fibers.