• Fibers and Polymers
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• v.7 no.4
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• pp.339-343
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• 2006

The aim of this paper is to improve moisture regain of PET fabrics using a lipase treatment. Effects of nine lipase sources, lipase activator and nonionic surfactant on moisture regain of PET fabrics are examined. Moisture regains of lipase-treated samples improve by two times in average compared with untreated and buffer-treated samples. Alkaline treatment creates larger pitting by more aggressive attack into fiber which is proved by SEM and water contact angle measurement. Moisture regain by alkaline treatment ($0.568%{\pm}0.08$) does not improve. However, lipase-treatment (L2 treatment) improves moisture regain up to 2.4 times ($1.272%{\pm}0.05$). Although lipase treatment is more moderate than alkaline treatment, lipase hydrolysis on PET fabrics improves moisture regain, efficiently. K/S values improved confirm that carboxyl and hydroxyl groups are produced on the surface of PET fabrics by lipase hydrolysis. Moisture regain and dyeability improve by lipase hydrolysis on PET fabrics.

• Journal of Aquaculture
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• v.18 no.4
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• pp.245-251
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• 2005

This study was investigated the condition of their maximum activity to assay the enzymes of rotifer, Brachionus rotundiformis의 $\alpha$-amylase, total alkaline Protease, trypsin and TG-lipase activities of rotifer were higher and more sensitive in phosphate-NaOH buffer than Tris-HCl buffer. $\alpha$-amylase, trypsin and TG-lipase activities were appeared the maximum at pH 8.0, and total alkaline protease activity showed the maximum activity at pH 7.0. $\alpha$-amylase activity showed the highest activity at $40^{\circ}C$, and total alkaline protease and trypsin activities were assayed the highest at $55{\~}60^{\circ}C$. However, TG-lipase activity was appeared the highest at $25{\~}30^{\circ}C$. The optimum substrate concentration of enzyme activity of a-amylase, total alkaline protease, rypsin and TG-lipase were $3.5\%$ starch, $\0.6%$ azo-casein, $87.5{\mu}M$ BApNA and 81.2 mM olive oil, respectively. The optimum reaction time of enzyme activity of $\alpha$-amylase, total alkaline protease, trypsin and TG-lipase were increased up to 40, 60, 30 and 25 min., respectively. The data obtained in this study could be used for the digestive enzyme research of rotifer, B. rotundiformis.

• Journal of Applied Biological Chemistry
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• v.50 no.2
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• pp.46-51
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• 2007

Lipases are industrially useful versatile enzymes that catalyze numerous different reactions. Among lipases functioning under extreme conditions, alkaline lipase is useful in detergent industry. Lipase from yeast strain Yarrowia lipolytica NRRL Y-2178 was most active under alkaline condition, and initial medium pH for most lipase production was also alkaline [Lee et al., 2007, J Microbiol Biotechnol, 17(6)]. High lipase production was achieved using Y. lipolytica NRRL Y-2178. Optimal incubation time for lipase production at $25^{\circ}C$ was 72 h. Optimal temperature, when incubated for 72 h, was $27.5^{\circ}C$. Lipase production but not cell growth was very sensitive to concentrations of glucose and glycerol as efficient carbon sources, showing optimal concentrations of 1.0 and 1.5% (w/v), respectively. Lipase production was highly stimulated by $Ca^{2+},\;K^+,\;and\;Na^+$, but was inhibited by $Co^{2+},\;Cu^{2+},\;Mn^{2+},\;Na^+,\;and\;Fe^{2+}$. Maximum lipase production at 0.1 mM $Ca^{2+}$ for 72 h incubation at $27.5^{\circ}C$ was 649 units/mL.

• Journal of Microbiology and Biotechnology
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• v.25 no.6
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• pp.845-855
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• 2015

The present study describes the gene cloning and high-level expression of an alkaline and thermostable lipase gene from Trichosporon coremiiforme V3. Nucleotide analysis revealed that this lipase gene has an open reading frame of 1,692 bp without any introns, encoding a protein of 563 amino acid residues. The lipase gene without its signal sequence was cloned into plasmid pPICZαA and overexpressed in Pichia pastoris X33. The maximum lipase activity of recombinant lipase was 5,000 U/ml, which was obtained in fed-batch cultivation after 168 h induction with methanol in a 50 L bioreactor. The purified lipase showed high temperature tolerance, and being stable at 60℃ and kept 45% enzyme activity after 1 h incubation at 70℃. The stability, effects of metal ions and other reagents were also determined. The chain length specificity of the recombinant lipase showed high activity toward triolein (C18:1) and tripalmitin (C16:0).

• Microbiology and Biotechnology Letters
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• v.21 no.3
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• pp.239-246
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• 1993

Producing an extracellular alkaline lipase, this isolate JM123 was identified as a Pseudomonas aeruginosa strain from the results of the analyses of its morphological, biochemical and physiological properties. This strain showed the highest productivity of alkaline lipase when grown at pH 9.0 and 30C for 13-20 hours in the medium of 2% starch, 1% soytone, 0.5% peptone and 1% MgSO4.7H2O. However, this enzyme was greatly repressed when grown in the glucose containing medium. The culture broth was fractionated by the order of the ammonium sulfate precipitation, Sephadex G-200 gel filtration, DEAE-cellulose column chromatography, and Sephadex G-150 gel filtration.

• Microbiology and Biotechnology Letters
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• v.22 no.3
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• pp.271-276
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• 1994

The strain S4-14 which produced alkaline lipase and had resistance against linear alkylbenzene sulfonate was isolated from soil or water samples. The isolated strain S4-14 was identified a species belong to Pseudomonas. Alkalin lipase secreted by Pseudomonas sp. S4-14 was purified by ammonium sulfate precipitation procedure follwed by DEAE-Cellulose, DEAE-Sepharose and gel filtration chromatohraphies with 995.15 U/mg protein and 16.1% yield. The molecular weight of the enzyme was estimated to be 65,000 dalton by SDS-PAGE. The optimum pH and temperature of the purified enzyme was 10.5 and 45$\circ $C, respectively. The emzyme was stable at 45$\circ $C for 1 hr and in a pH range from 8.0 to 12.0 for 24 hr at 4$\circ $C. The activity of lipase was enhanced by Ca$^{2+}$ while inhibited strongly by Pb$^{2+}$, Zn$^{2+}$ or Fe$^{3+}$. The activity of lipase was inactivated about 50~60% in the presence of 50 mg/l linear alkylbenzene sulfonate, $\alpha $-olefin sulfonate, alcohol ethoxylate or perborate.

• Microbiology and Biotechnology Letters
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• v.23 no.6
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• pp.695-701
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• 1995

An alkaline lipase producing bacteria was isolated from soil and identified as Serratia liquefaciens AL-11. from the results of analysis of its morphological, biochemical and physiological properties. This strain showed the highest productivity of alkaline lipase when grown at pH 9.0 and 30$\circ$C for 42 hours in the medium of 1% peptone, 0.5% tryptone, 0.9% yeast extract, 1% starch, 1% tween 80, 0.05% CaCl$_{2}$ and 0.05% NaCl. The enzyme was purified by ammonium sulfate treatment, Sephadex G-100 gel filtration and DEAE-Sephadex A-50 column chromatography. The specific activity of the purified enzyme was 27 unit/mg protein and the yield of enzyme activity was 61.3%. The homogeneity of the purified enzyme was verified by polyacrylamide gel disc electrophoresis. Molecular weight of the purified enzyme was estimated about 53,000 by sodium dodecyl sulfate- polyacrylamide gel electrophoresis. This enzyme is composed of 17 amino acids of which glycine, proline and glutamic acid were three miajor acids.

• Journal of Life Science
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• v.11 no.5
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• pp.457-463
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• 2001

A bacterial strain SC-22 which produced alkaline lipase was isolated from salf-fermented shrimps. Strains SC-22 was identified as Staphylococcus xylosus. An alkaline lipase excreted by Staphylococcus xylosus SC-22 was purified by ammonium sulfate predipitation and column chromatography on Sephadex G-100 and DEAE-Sephace. The specific activity of purified lipase was 756U/mg of protein with 17.2% yield. The approximate molecular weight of the purified enzyme was 47 kDa. The partially purified lipase preparation had and optimum temperature of 4$0^{\circ}C$, an optimum pH of 8.0, and a stable of 5~10. Lipase activities were enhanced by salt ions such as $Ca^{2+}$, $Mg^{2+}$,N $a^{2+}$ while inhibited remarkably by heavy metal ions, C $u^{2+}$ and P $b^{2+}$.EX> 2+/.

• Journal of Microbiology and Biotechnology
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• v.17 no.6
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• pp.1054-1057
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• 2007

Lipases are industrially useful versatile enzymes that catalyze numerous different reactions including hydrolysis of triglycerides, transesterification, and chiral synthesis of esters under natural conditions. Although lipases from various sources have been widely used in industrial applications, such as in food, chemical, pharmaceutical, and detergent industries, there are still substantial current interests in developing new microbial lipases, specifically those functioning in abnormal conditions. We screened 17 lipase-producing yeast strains, which were prescreened for substrate specificity of lipase from more than 500 yeast strains from the Agricultural Research Service Culture Collection (Peoria, IL, U.S.A.), and selected Yarrowia lipolytica NRRL Y-2178 as a best lipase producer. This report presents new finding and optimal production of a novel extracellular alkaline lipase from Y. lipolytica NRRL Y-2178. Optimal culture conditions for lipase production by Y. lipolytica NRRL Y-2178 were 72 h incubation time, $27.5^{\circ}C$, pH 9.0. Glycerol and glucose were efficiently used as the most efficient carbon sources, and a combination of yeast extract and peptone was a good nitrogen source for lipase production by Y. lipolytica NRRL Y-2178. These results suggested that Y. lipolytica NRRL Y-2178 shows good industrial potential as a new alkaline lipase producer.

• Microbiology and Biotechnology Letters
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• v.19 no.1
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• pp.57-63
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• 1991

A strain J-19 was isolated from soil, produced lipase which has resistant against alkali and linear alkylbenzene sulfonate. The strain was identified as Pseudornonns sp.. The enzyme was purified by ammonium sulfate precipitation, DEAE-Sephadex and Sephadex G- 100 column chromatography. The specific activity of the purified enzyme was 35 unit/mg protein and the yield of enzyme activity was 17%. The purified enzyme showed a single band on polyacrylamide disc gel electrophoresis. Mo1ecul;tr weight of the purified enzyme was estimated about 36,000 by Sephadex GI00 gel filtration and SDS-polyacrylarnide gel electrophoresis. The optimum pH and temperature were pH 10.0 and $30^{\circ}C$, respectively. Activity of the purified enzyme was increased 2-fold by the addition of 0.1% linear alkylbenzene sulfonate and 2.5- fold by the addition of 0.05% Tide. This enzyme remained stable from pH 8.0 to 10.0 and stable up to $40^{\circ}C$.