• Biotechnology and Bioprocess Engineering:BBE
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• v.10 no.4
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• pp.329-333
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• 2005

This study was designed to investigate the stability of a lipase fused with a cellulose­binding domain (CBD) to cellulase. The fusion protein was derived from a gene cluster of a CBD fragment of a cellulase gene in Trichoderma hazianum and a lipase gene in Bacillus stearother­mophilus L1. Due to the CBD, this lipase can be immobilized to a cellulose material. Factors affecting the lipase stability were divided into the reaction-independent factors (RIF), and the re­action-dependent factors (RDF). RIF includes the reaction conditions such as pH and tempera­ture, whereas substrate limitation and product inhibition are examples of RDF. As pH 10 and $50^{\circ}C$ were found to be optimum reaction conditions for oil hydrolysis by this lipase, the stability of the free and the immobilized lipase was studied under these conditions. Avicel (microcrystal­line cellulose) was used as a support for lipase immobilization. The effects of both RIF and RDF on the enzyme activity were less for the immobilized lipase than for the free lipase. Due to the irreversible binding of CBD to Avicel and the high stability of the immobilized lipase, the enzyme activity after five times of use was over $70\%$ of the initial activity.

• Applied Biological Chemistry
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• v.23 no.1
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• pp.52-57
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• 1980

This study was conducted to clarify the mode of action and the positional specificity of Trichosporon cutaneum lipase during the course of hydrolysis of triolein and monoolein mixture by thin-layer chromatography. 1. The hydrolytic activity of the lipase to oleyl glycerides was in the order of triolein>diolein>monoolein. 2. Both of triolein and diolein were hydrolyzed by the lipase at high and almost the same rate. 3. The hydrolysis of monoolein by the lipase was very slow compared to the other two oleyl glycerides. 4. This lipase appeared to have a very low specificity toward the outer chains of triolein.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2001.06a
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• pp.163-164
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• 2001

A number of bacterial species produce extracellular lipases. Among them, many lipase genes have been cloned and sequenced. A comparison of primary sequences revealed only very limited sequence homology among them. Based on the sequence homologies and molecular sizes (Mr), bacterial lipases were classified into four discrete groups. From soil samples taken around Taejon, five different lipase-producing bacteria were isolated; Proteus vulgaris K80, Bacillus stearothermophilus Ll, B. pumilus B26, Staphylococcus haemolyticus L62, S. aureus B56. Nucleotide sequence analysis showed that Staphylococcus lipase genes (L62 and B56) composed of pre-pro-mature parts, Bacillus lipase genes (Ll and B26) pre-mature parts, and Proteus lipase gene (K80) mature part only. In addition, the molecular sizes of their mature parts were quite different from 19,000 to 45,000. Finally, they had very little homology (less than 20％) in their amino acid sequences. Judging from the above results, lipase K80 belonged to bacterial lipase Group I, lipase L1 and lipase B26 Group III, and lipase L62 and lipase B56 Group IV. This diversity in their primary structures was also reflected in their enzymatic properties; temperature effects, pH effects, substrate specificity, detergent effects, and so on.

• Journal of the Korean Society of Clothing and Textiles
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• v.24 no.2
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• pp.205-213
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• 2000

This study investigated the effect of mixing protease and lipase on detergency. The detergency of protein soiled, oil soiled and protein-oil soiled cloths and the relative hydrolytic activity of enzymes were examined. The protease-lipase added detergent solution was most effective for the removal of protein in protein-oil soiled cloths. This is because the lipase removed the protein that was physically bound to oil as well as the protease removed the protein. The protease added detergent solution was second effective, the lipase added detergent solution was third effective, and the detergent solution without protease and lipase was the least effective. The protease-lipase added detergent solution was also most effective in the oil removal from protein-oil soiled cloths. Unlike in protein removal, however, the protease added detergent solution was more effective in oil removal than the lipase added detergent solution. This is because the removal of oil bound to protein by protease was more effective than the removal of oil by lipase. In soiling-washing cycles, however, the effects of lipase increased, and as a result, the detergency of protease added detergent solution and the lipase added detergent solution became similar.

• 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.

• 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 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.3 no.1
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• pp.1-6
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• 1975

The excellent strain $K_{52}$ for producing lipase was selected among 215 strains of Rhizopus sp. isolated from soil and other natural sources. The results investigated of microbiological characters and conditions for producing lipase Ivere summarized as follows： (1) Strain $K_{52}$ was similar to Rhizopus delemar in microbiological character. (2) The lipase activity was most vigorous after 48 hours in wheat bran culture, 96 hours in surface culture and 72 hours in shaking colure. (3) Surface culture was more suitable than in shaking culture for producing lipase. (4) In the case of wheat bran culture, producing of lipase was vigorous after 48 hours of culure period (3,800u/g) . (5) The optimum temperature for producing lipase was 3$0^{\circ}C$ both in wheat bran culture and in surfase culture.

• Microbiology and Biotechnology Letters
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• v.48 no.2
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• pp.167-178
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• 2020

Lipase-producing fungi have been isolated from environments containing lipids. The non-dairy creamer industrial waste has a high amount of lipids so it is a potential source for the isolation of lipase-producing fungi. However, the study of fungi that secrete lipase from this industrial waste has not been reported. The purpose of this study was to obtain lipase-producing filamentous fungi from non-dairy creamer industrial waste. Mineral salt and potato dextrose agar were used as media for the isolation process. The qualitative screening was conducted using phenol red agar medium and the quantitative screening using broth medium containing glucose and olive oil. Isolates producing the highest amounts of lipase were identified with molecular methods. We found that 5 out of 19 isolated filamentous fungi are lipase producers. Further analysis showed that isolate Ms.11 produced the highest amount of lipase compared to others. Based on ITS sequence Ms.11 was identified as Aspergillus aculeatus. The lipase activity in medium containing 1% glucose + 1% olive oil at pH 7.0 and 30℃ after 96 and 120 h of incubation was 5.13 ± 0.30 U/ml and 5.22 ± 0.59 U/ml, respectively. The optimum lipase activity was found at pH 7.0, 30℃ and using methanol or ethanol in the reaction tube. Lipase was more stable at 20-30℃ and maintained 85% of its activity. It was concluded that isolate Ms.11 is a potential source of lipase that catalyzes transesterification reactions. Further studies are required to optimize lipase production to make the strain suitable for industry purposes.

• Journal of Microbiology and Biotechnology
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• v.23 no.5
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• pp.661-667
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• 2013

Lipase-producing bacterial strains were isolated from Antarctic soil samples using the tricaprylin agar plate method. Seven strains with relatively strong lipase activities were selected. All of them turned out to be Bacillus pumilus strains by the 16S rRNA gene sequence analysis. Their corresponding lipase genes were cloned, sequenced, and compared. Finally, three different Bacillus pumilus lipases (BPL1, BPL2, and BPL3) were chosen. Their amino acid sequence identities were in the range of 92-98% with the previous Bacillus pumilus lipases. Their optimum temperatures and pHs were measured to be $40^{\circ}C$ and pH 9. Lipase BPL1 and lipase BPL2 were stable up to $30^{\circ}C$, whereas lipase BPL3 was stable up to $20^{\circ}C$. Lipase BPL2 was stable within a pH range of 6-10, whereas lipase BPL1 and lipase BPL3 were stable within a pH range of 5-11, showing strong alkaline tolerance. All these lipases exhibited high hydrolytic activity toward p-nitrophenyl caprylate ($C_8$). In addition, lipase BPL1 showed high hydrolytic activity toward tributyrin, whereas lipase BPL2 and lipase BPL3 hydrolyzed tricaprylin and castor oil preferentially. These results demonstrated that the three Antarctic Bacillus lipases were alkaliphilic and had a substrate preference toward short- and medium-chain triglycerides. These Antarctic Bacillus lipases might be used in detergent and food industries.