• Biotechnology and Bioprocess Engineering:BBE
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• 제10권4호
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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.

• 한국의류학회지
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• 제24권2호
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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.

• 한국식품과학회지
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• 제17권2호
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• pp.60-64
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• 1985

미생물에서 추출된 lipase를 유지방분해에 이용하기 위한 기초연구로서 Rhizopus delemar, Mucor sp. 및 Candida cylindracea에서 추출된 3중의 lipases를 유지방분해에 적합한 반응조건을 설정하고, 이들의 반응 특이성을 연구한 결과는 다음과 같다. 최적온도 및 최적pH는 Rhizopus delemar lipases가 $45^{\circ}C$, pH5.6 Mucor sp. lipases가 $35^{\circ}C$, pH7.5였으며, Candida cylindracea lipase는 $35^{\circ}C$, pH 7.0 이었다. 유지방에 대한 적정효소농도는 3종의 lipase 모두 $600{\sim}800\;units/ml$였다. 적정기질농도는 효소의 종류에 관계없이 유지방함량 20%였으며, 이들의 Km값은 R. delemar lipase가 6.06%, M sp. lipase가 7.69%, Can. cylindracea lipase가 7.99%였다. 반응시간에 따른 반응율을 조사한 결과 R. delemar lipase, M. sp. lipase, Can. cylindracea lipase순으로 높았으며 반응시간이 진행됨에 따라 저급지방산의 분해율이 높아졌으며, 반응 8시간에서는 R. delemar lipase는 butylic acid, M. sp. lipase는 palmitic acid, Can. cylindracea lipase는 Capric acid의 함량이 높았다.

• 한국의류학회지
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• 제33권7호
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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.

• 한국식품영양과학회지
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• 제20권1호
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• pp.40-45
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• 1991

The release of hepatic triglyceride lipase from cultured rat hepatocytes and its hormonal regulation were studied. The activity of lipase released into the medium in the presence of heparin was increasing during 24 hours on the 2nd of culture while this was 10% in the absence of heparin as compared with the lipase activity in the presense of heparin. When hepatocytes were cultured with anti-hepatic triglyceride lipase lgG the lipase activity was supp-ressed by 92% The results suggest that the enzyme relaeased into culture medium is identical to hepatic triglyceride lipase which can be released only in the presence of heparin the model of release being similar to that of lipoprotein lipase from adipocytes. The addition of monensin to the medium resulted in The inhibition of lipase secretion by 61% Insulin enhanced lipase activity only 20% whereas dexamethasone suppressed the activity by 44% These data inidica-ted that hepatic triglyceride lipase is secreted and released from hepatocytes in the presence of heparin and its secretion is regulated by hormones.

• 한국미생물·생명공학회지
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• 제49권3호
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• pp.337-345
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• 2021

Lipase (triacylglycerol lipase, EC 3.1.1.3) is an enzyme capable of hydrolyzing triacylglycerol, to produce fatty acids and glycerol and reverse the reaction of triacylglycerol synthesis from fatty acids and glycerol through transesterification. Applications of lipase are quite widespread in the industrial sector, including in the detergent, paper, dairy, and food industries, as well as for biodiesel synthesis. Lipases by yeasts have attracted industrial attention because of their fast production times and high stability. In a previous study, a lipase-producing yeast isolate was identified as Zygosaccharomyces mellis SG1.2 and had a productivity of 24.56 U/mg of biomass. This productivity value has the potential to be a new source of lipase, besides Yarrowia lypolitica which has been known as a lipase producer with a productivity of 0.758 U/mg. Lipase production by Z. mellis SG1.2 needs to be increased by optimizing the production medium. The aims of this study were to determine the significant component of the medium for lipase production and methods to increase lipase production using the optimum medium. The two methods used for the statistical optimization of production medium were Taguchi and RSM (Response Surface Methodology). The data obtained were analyzed using Minitab 18 and SPSS 23 software. The most significant factors which affected lipase productivity were olive oil and peptones. The optimum medium composition consisted of 1.02% olive oil, 2.19% peptone, 0.05% MgSO₄·7H₂O, 0.05% KCl, and 0.2% K₂HPO₄. The optimum medium was able to increase the lipase productivity of Z. mellis SG1.2 to 1.8-fold times the productivity before optimization.

• 한국식품과학회지
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• 제17권2호
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• pp.75-80
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• 1985

Lipase를 유지분해에 이용하기 위한 기초연구로서 Candida cylindracea에서 추출된 lipase를 흡착법에 의해 고정화하고 그의 반응특이성을 본 결과는 다음과 같다. Lipase 흡착에 적합한 흡착제로는 silica gel이 선정되었으며, Silica gel 1.6g에 lipase 47.5 units를 $5^{\circ}C$, PH 7.0에서 100분간 흡착시키는 것이 좋았다. Silica gel에 고정화 시킨 lipase를 유지방과 olive oil의 분해에 적합한 최적온도 및 최적pH는 가용성효소와 비교시 $37^{\circ}C$, pH 7.0으로 변하지는 않았으나 활성의 범위는 넓어졌다. 또한 열안정성 및 pH안정성도 가용성 효소에 비하여 활성의 범위가 넓어졌다. 유지의 분해에 적합한 고정화 효소의 최적효소농도는 유지방의 경우 30g이었으며 올리브유의 경우 80g으로 선정하였다. 이 때 최적기질농도는 유지방 및 올리브유 모두 20%였다. 반응시간에 따른 반응률은 유지방을 이용하여 조사한 결과 가용성 효소는 반응 4시간까지는 급격한 분해를 나타냈으나 고정화 효소는 8시간 까지 급격한 증가를 나타내고 그 이상은 거의 일정하였다. 또한 유리되는 지방산의 profile은 가용성 효소와 비교시 capric acid의 생성은 모두 높았으며, myristic acid의 함량은 높고 butyic acid의 함량은 적었다.

• Journal of Microbiology and Biotechnology
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• 제26권1호
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• pp.80-88
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• 2016

The enzyme-catalyzed Henry reaction was realized using deep eutectic solvents (DESs) as a reaction medium. The lipase from Aspergillus niger (lipase AS) showed excellent catalytic activity toward the substrates aromatic aldehydes and nitromethane in choline chloride:glycerol at a molar ratio of 1:2. Addition of 30 vol% water to DES further improved the lipase activity and inhibited DES-catalyzed transformation. A final yield of 92.2% for the lipase AS-catalyzed Henry reaction was achieved under optimized reaction conditions in only 4 h. In addition, the lipase AS activity was improved by approximately 3-fold in a DES-water mixture compared with that in pure water, which produced a final yield of only 33.4%. Structural studies with fluorescence spectroscopy showed that the established strong hydrogen bonds between DES and water may be the main driving force that affects the spatial conformation of the enzyme, leading to a change in lipase activity. The methodology was also extended to the aza-Henry reaction, which easily occurred in contrast to that in pure water. The enantioselectivity of both Henry and aza-Henry reactions was not found. However, the results are still remarkable, as we report the first use of DES as a reaction medium in a lipase-catalyzed Henry reaction.

• Journal of Microbiology and Biotechnology
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• 제9권6호
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• pp.832-838
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• 1999

Two different types of lipases (lipase I and lipase II) secreted into culture medium by Rhizopus sp. L-I were purified using a hydrophobic chromatography and were partially characterized. Both enzymes were monomeric as revealed by SDS-PAGE and gel filtration. The molecular masses of the enzymes were identified as 45 kDa (lipase I) and 69 kDa (lipase II). The isoelectric points were estimated to be 3.6 and 5.2 for lipase I and lipase II, respectively. pH and temperature activity optima for lipase I were as 7.5 and $50^{\circ}C$, respectively, whereas the corresponding parameters for lipase II were 6.0 and $45^{\circ}C$. The amino terminal sequences of lipase I and lipase II, determined by Edman degradation, were found to be Leu-Val-Met-Ile-Gln-Arg and Leu-Val-Met-Lys-Gln-Arg, respectively. By western blotting analysis, the two lipases were found to have a common antigenic determinant. Immuno-electron cytochemistry conducted with polyclonal anti-lipase I antibody indicated the enzyme located in both the periplasm and the adjacent vesicles of fungal hyphae. Fortunately, the sites on the cell envelope where lipase was exported into the culture medium was also identified.

• 한국식품과학회지
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• 제8권1호
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• pp.33-41
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• 1976

1. 유기질소원(有機窒素源)으로는 soybean meal, 무기질소원(無機窒素源)으로는 $(NH_4)_2SO_4$가 lipase생산(生産)에 가장 효과(效果)이었다. 2. 배양중(培養中) 배지(培地)의 pH저하(低下)를 이르키는 xylose, glucose, fructose, galactose, mannose, maltose, soluble starch, dextrin을 탄소원(炭素源)으로 첨가(添加)하였을 때 lipase 생산(生産)이 심(甚)하게 저해(沮害)되었다. sucrose는 lipase생산(生産)을 저해(沮害)하지 않았으나 첨가효과(添加效果)는 인정(認定)되지 않았다. 3. 인산염(燐酸鹽)으로서는 $K_2HPO_4$, 마그네슘염(鹽)으로서는 $MgSO_4{\cdot}7H_2O$가 lipase생산(生産)에 가장 효과적(效果的)이었다. 4. Olive유(油), 대두유(大豆油) 및 야자유(油)의 첨가(添加)는 lipase생산(生産)을 증가(增加)시켰으며 1% olive유(油) 첨가시(添加時) lipase생산(生産)이 50% 증가(增加)되었다. 5. yeast extract $0.05{\sim}0.07%$첨가시(添加時) lipase생산(生産)이 약간 증가(增加)되었다. 6. 본균(本菌)의 lipase생산(生産)에 가장 적합(適合)한 배지(培地)는 soybean meal 2%, $K_2HPO_4$ 0.5%, $(NH_4)_2SO_4$ 0.1%, $MgSO_4{\cdot}7H_2O$ 0.05%, yeast extract 0.05%, olive유(油) 1%의 조성(組成)의 것으로서 최적배양조건하(最適培養條件下)에서 48시간(時間) 배양시(培養時)에 lipase생산(生産)이 최고(最高)에 도달(到達)하였다.