• Journal of Microbiology and Biotechnology
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• v.22 no.1
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• pp.84-91
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• 2012

Two staphylococcal lipases were obtained from Staphylococcus epidermidis S2 and Staphylococcus aureus S11 isolated from sebaceous areas on the skin of the human face. The molecular mass of both enzymes was estimated to be 45 kDa by SDS-PAGE. S2 lipase displayed its highest activity in the hydrolysis of olive oil at $32^{\circ}C$ and pH 8, whereas S11 lipase showed optimal activity at $31^{\circ}C$ and pH 8.5. The S2 lipase showed the property of cold-adaptation, with activation energy of 6.52 kcal/mol. In contrast, S11 lipase's activation energy, at 21 kcal/mol, was more characteristic of mesophilic lipases. S2 lipase was stable up to $45^{\circ}C$ and within the pH range from 5 to 9, whereas S11 lipase was stable up to $50^{\circ}C$ and from pH 6 to 10. Both enzymes had high activity against tributyrin, waste soybean oil, and fish oil. Sequence analysis of the S2 lipase gene showed an open reading frame of 2,067 bp encoding a signal peptide (35 aa), a pro-peptide (267 aa), and a mature enzyme (386 aa); the S11 lipase gene, at 2,076 bp, also encoded a signal peptide (37 aa), pro-peptide (255 aa), and mature enzyme (399 aa). The two enzymes maintained amino acid sequence identity of 98-99% with other similar staphylococcal lipases. Their microbial origins and biochemical properties may make these staphylococcal lipases isolated from facial sebaceous skin suitable for use as catalysts in the cosmetic, medicinal, food, or detergent industries.

• Applied Biological Chemistry
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• v.42 no.2
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• pp.105-110
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• 1999

Acetobacter sp. were isolated from persimmon vinegar. We studied about conditions of Aloe vinegar fermentation by an isolated strain and inhibitory effect against lipase activity. Strains DS-118 was strictly aerobic, motile, gram negative, non-spore-forming and short rod shaped. It reacted positively in catalase test, was oxidase test negative, was ureas negative, was produced acetic acid from alcohol. On the basis of these results, it was identified as a strain of Acetobacter sp. In the preparation of Aloe vinegar, optimun initial alcohol concentration, acidity, and fermentation temperature were 10%, $3{\sim}4%$ and $25^{\circ}C$, respectively. The major organic acid in Aloe vinegar was acetic acid (12%), but malic acid and ${\delta}-galactronic$ acid were also present in trace. The Aloe vinegar(acidity : 12%) inhibited lipase activity and it's $IC_{50}$ was 43%.

• Journal of Applied Biological Chemistry
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• v.60 no.3
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• pp.235-239
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• 2017

The objective of the present study was to evaluate in vitro antioxidant activity, antioxidant content and pancreatic lipase inhibitory activities of Makgeolli supplemented with 0, 1, 2, and 4% (w/v) Jeju camellia mistletoe during fermentation. Total phenolic and flavonoid contents tended to increase as content of Jeju camellia mistletoe increased. Supplementation with Jeju camellia mistletoe resulted in a significant increase in the scavenging capacities of 1,1-diphenyl-2-picrylhydrazyl, hydrogen peroxide, nitric oxide and superoxide anion radicals, and reducing power activity. Moreover, pancreatic lipase inhibitory activity was significantly elevated by Jeju camellia mistletoe addition. These results suggest that Jeju camellia mistletoe is considered to be a good material to improve antioxidant and pancreatic lipase inhibitory activities of makgeolli.

• Journal of Life Science
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• v.16 no.2 s.75
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• pp.328-332
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• 2006

The possible presence of inhibitors of pancreatic lipase (tricaylglycerol acylhydrolase EC 3.1.1.3) was screened from Korean traditional edible or medicinal herbs. Among tested herbs, Arecae pericarpium, Mucunae Caulis, Rhus javanica, Thujae orientalis were shown to have strong inhibitory effect against pancreatic lipase. Thujae orientalis was finally selected as a candidate for pancreatic lipase inhibitor. The extract of Thujae orientalis was showed selective inhibition on porcine pancreatic lipase activity. Active inhibitors, TF-1, TF-2, TF-3, were purified from an extract of Thujae orientalis, using chloroform extraction, followed by successive chromatography in silica gel and LH-20 and high performance liquid chromatography (HPLC). The $IC_{50}$ values of TF-1, TF-2, TF-3 and orlistat were 44.7, 98.7, 46.1 and $27.6{\mu}g/ml$, respectively. And also the TF-2 and orlistat were shown to be inhibitory effect on the differentiation of preadipocyte NIH-3T3 L1 cells at a concentration of $10{\mu}g/ml$.

• Asian-Australasian Journal of Animal Sciences
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• v.30 no.2
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• pp.192-197
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• 2017

Objective: The study was conducted to evaluate the stability of commercial coated lipase (CT-LIP) in vitro. Methods: The capsules were tested under different conditions with a range of temperature, pH, dry heat treatment and steaming treatment, simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) in this work, respectively. Free lipase (uncoated lipase, UC-LIP) was the control group. Lipase relative activities measured in various treatments were used as a reference frame to characterize the stability. Results: The lipase activities were decreased with increasing temperatures (p<0.05), and there was a markedly decline (p<0.01) in lipase comparative activities of UC-LIP at $80^{\circ}C$ compared with CT-LIP group. Higher relative activities of lipase were observed in CT-LIP group compared with the free one under acidic ambient (pH 3 to 7) and an alkaline medium (pH 8 to 12). Residual lipase activities of CT-LIP group were increased (p<0.05) by 5.67% and 35.60% in dry heat and hydrothermal treatments, respectively. The lipase relative activity profile of CT-LIP was raised at first and dropped subsequently (p<0.05) compared with constantly reduced tendency of UC-LIP exposed to both SGF and SIF. Conclusion: The results suggest that the CT-LIP possesses relatively higher stability in comparison with the UC-LIP in vitro. The CT-LIP could retain the potential property to provide sustained release of lipase and thus improved its bioavailability in the gastrointestinal tract.

• The Korean Journal of Food And Nutrition
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• v.8 no.3
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• pp.192-198
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• 1995

For the production of EMC, various professes and lipases were used to hydrolyse cheese sulk. The optimal conditions of various proteases were as follows, pronase-3$0^{\circ}C$, p14 7.0, pancreatln-4$0^{\circ}C$, pH 8.0, pacific protease-3$0^{\circ}C$, pH 7.0 and protease from Asp. sp. -5$0^{\circ}C$, pH 8.0. The optimal conditions of various lipases were as follows ; pancreatic lipase-5$0^{\circ}C$, pH 8.0, palatase ML-5$0^{\circ}C$, pH 7.0 and lipase form Candida -4$0^{\circ}C$, pH U.0. After hydrolysation under optimal conditions, the amounts of free amino acid and free fatty ac14 were increased with reaction time. Hydrolysates of pacific protease and pronase were showed high amount of free amino acid(0.67mg/ml and 0.74mg/ml). Especially EMC had high amount of glutamic acid and leucine. Lipase from Candida cylindracea produced high amount of free fatty acid (24.63 mg/ml) Butyric acrid, palmitic acid, stearic acid and oleic acid among free fatty acids were showed high amounts. Sensory evaluation of various MC were tasted nth 8 panelist. EMC produced with pancreatic lipase was most bitterness and EMC produced with palatase ML was best acceptable cheese flavor.

• Analytical Science and Technology
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• v.29 no.3
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• pp.105-113
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• 2016

The present study investigated the immobilization of lipases on silica nanoparticles and silica-coated magnetite nanoparticles as supports with a functional group to enhance the stability of lipase. The influence of functional groups, such as the epoxy group and the amine group, on the activity and stability of immobilized lipase was also studied. The epoxy group and the amino group were introduced onto the surface of nanoparticles by glycidyl methacrylate and aminopropyl triethoxysilane, respectively. Immobilized Candida rugosa lipase on silica nanoparticles and silica-coated magnetite nanoparticles with a functional group showed slightly lower initial enzyme activities than free enzyme; however, the immobilized Candida rugosa lipase retained over 92 % of the initial activity, even after 3 times reuse. Lipase was also immobilized on the silica-coated magnetite nanoparticles by cross-linked enzyme aggregate (CLEA) using glutaraldehyde and covalent binding, respectively, were also studied. Immobilized Candida rugosa lipase on silica nanoparticles and silica-coated magnetite nanoparticles by CLEA and covalent binding showed higher enzyme activities than free enzyme, while immobilized Candida rugosa lipase retained over 73 % of the initial activity after 5 times reuse.

• Food Science of Animal Resources
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• v.30 no.5
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• pp.764-772
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• 2010

Staphylococcus aureus lipase is regarded as a virulence factor. The response of lipase activity to various factors can provide important insights concerning the prevention of S. aureus during meat fermentation. This study was conducted to evaluate the main effects of nutrients used in culture media, and their combined effects on the inhibition of lipase activity and cell growth of pathogenic S. aureus SK1593 isolated from fermented pork meat. A Plackett-Burman design was used to evaluate the main effects of variables, including olive oil, soybean oil, grapeseed oil, sesame oil, $CuSO_4$, $MgCl_2$, $KNO_3$, $CaCl_2$, and KCl. Significant negative effects on lipase activity were detected with soybean oil, grapeseed oil, $KNO_3$, and $CaCl_2$. Additionally, these nutrients were further selected as variables for the investigation of their combined effect on lipase activity, via response surface methodology. In order to confirm the regression model, a situation that only inhibits lipase activity was simulated. The predicted lipase activity and cell growth of the simulated situation were 14.0 U/mL and $9.6\;{\log}_{10}$ (CFU/mL), respectively, and the estimated value of those in the same medium showed 15.14 U/mL and $9.4\;{\log}_{10}$(CFU/mL) respectively. The lipase activity of the simulated medium was inhibited approximately 5-fold as compared to the basal medium, but no significant differences in cell counts were noted to exist between the basal and simulated media. These results suggest that soybean oil, grapeseed oil, $KNO_3$, and $CaCl_2$ can be used to inhibit the growth of pathogenic S. aureus during the process of meat fermentation.

• Journal of the Korean Ceramic Society
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• v.35 no.9
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• pp.958-968
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• 1998

Porous silica ceramics were prepared using DCCA(Drying Control Chemical Additives) Such as uncharged polymer(Polyethylene glycol) and protein (Lipase) under H2O/Low-grade TEOS=10 C2H5OH/Low-grade TEOS=1 HC1/Low=grade TEOS=0.01 After Plain which doesn't added DCCA and samples of 11 sorts which varied molecular weight of PEG(Mw=600, 1000, 2000) quantity of Lipase and concentration of wat-er were synthesized gellation time and thermal analysis were investigated. After heat-treated at 600, cry-stal structures analyses of SiO2 polymer and characteristics of pores were investigated. Gellation time was retarded about 2-6 times as compared with plain resulting in addition of DCCA and crystal structures ex-hibited amorphous state. Moreover as increase of water a short gellation time was obtained. The samples added PEG showed increase of specific surface areas up to 20-40% and had micropores while those of Lipase were decreased about 90% and showed broad pore size distribution.

• Journal of Life Science
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• v.5 no.4
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• pp.155-161
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• 1995

The effects of substrate concentration, enzyme concentration, reaction temperature, and water content were investigated in intramolecular esterification. This study used cyclohexane as organic solvent, power lipase as enzyme, and benzyl alcohol and octanoic acid as substrate. The initial reaction rate was found to be proportional to enzyme concentration; followed Michaelis-Menten equation for octanoic acid; and was inhibited by benzyl alcohol . The observed initial reaction rate first increased, then decreased with increasing reaction temperature, giving rise to the maximum rate at 20$\circ$. The drop in the reaction rate at higher temperature was to partition equilibrium change of substrate between organic solvent and hydration layer of enzyme molecule in addition to the deactivation by enzyme denaturation. Water layer surrounding enzyme molecule seemed to activate in organic solvent and the realistic reaction was done in the water layer. In the enzymatic reaction in organic solvent, the initial reaction rate was influenced by partition quilibrium of substrate, so the optimum condition of substrate concentration, enzyme concentration, reaction temperature, and water content would give a good design tool.