• 제목/요약/키워드: Lipase AS

검색결과 676건 처리시간 0.022초

Deactivation kinetics of C. rugosa lipase

  • 손현수;이준식
    • 한국미생물생명공학회:학술대회논문집
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    • 한국미생물생명공학회 1986년도 추계학술대회
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    • pp.523.1-523
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    • 1986
  • To extend the spectrum of enzyme utilization in the organic solvent system, C. rugosal lipase was selected as a model enzyme because its substrate is soluble to organic solvent. One of the serious disadvantages in this system was the deactivation of the lipase. The pattern of lipase deactivation was the biphasic model. The activation energies for the deactivation were 14.05${\times}$10$^4$ KJ/Kg mole in the first phase and 3.59 ${\times}$ 10$^4$ KJ/mole in the second phase. The several factors were studied for their influences on the pattern of deactivation. Iso-octane as organic solvent influenced more on the first phase than the second phase. Urea as the reagent affecting boty hydrophobic interaction and hydrogen bond of enzyme also influencea more on the first phase. And the optimum pH for the activity was not correlated to that of the stability.

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APPLICATION OF STABLE EMULSIONS TO LIPASE IMMOBILISED MEMBRANE REACTORS FOR KINETIC RESOLUTION OF RACEMIC ESTERS

  • Giorno, Lidietta;Na, Li;Drioli, Enrico
    • 한국막학회:학술대회논문집
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    • 한국막학회 2003년도 The 4th Korea-Italy Workshop
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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.

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A Convergent Synthesis of Bis-2-oxo Amide Triacylglycerol Analogues as Potent Lipase Inhibitors Using Acyl Cyanophosphorane Methodology

  • Lee, Kie-Seung
    • Bulletin of the Korean Chemical Society
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    • 제23권2호
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    • pp.351-354
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    • 2002
  • A number of bis-2-oxo amide triacylglycerol analogues, a recently reported potent human gastric lipase inhibitor and its new analogues, have been prepared starting from 1,3-dibromo-2-propanol utilizing acyl cyanophosphorane methodology as a key step in a convergent manner. The key coupling reaction has been accomplished at -$78^{\circ}C$ between 1,3-diamino-2-propanol derivative and the labile diketo nitriles, derived from acyl cyanotriphenylphosphoranes upon oxidizing with $O_3$, under mild condition in moderate yields.

Detection and Determination of Lipase Activity

  • Lee, Seoung-Yong;Rhee, Joon-Shick
    • Journal of Microbiology and Biotechnology
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    • 제4권2호
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    • pp.85-94
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    • 1994
  • Lipase (triacylglycerol hydrolase, EC 3.1.1.3) is able to catalyze the hydrolysis of ester bonds of triacylglycerols at the interface between aqueous phase and organic phase containing substrate. With the rapid development of lipid biotechnology, lipase-catalyzed hydrolysis of lipids has a great concern from the industrial point of view. Owing to the reversible nature of the lipase, the reactions are also applied for glyceride synthesis, interesterification and resolution of racemic mixtures into optically active alcohols or acids. For all applications of the lipases, a reliable method for the determination of enzyme activity is required. Precise quantitative determination of its activity is essential as the basis of research and development of the bioprocess involving the enzyme. This article reviews the existing literature on the detection and determination of lipase activity from microbial, mammalian and plant sources.

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Trichosporon Cutaneum 의 Lipase 에 관(關)한 연구(硏究) -제(第) 1 보(報) Lipase 생산균(生産菌)의 분리(分離) 및 동정(同定)- (Studies on the Lipase of Trichosporon cutaneum -Part 1. Isolation and Identification of Lypolytic Microorganisms-)

  • 김성열
    • Applied Biological Chemistry
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    • 제15권3호
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    • pp.221-227
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    • 1972
  • (1) Olive oil을 유일탄소원(唯一炭素源)으로하는 배지(培地)를 사용(使用)하여 공기(空氣) 및 토양중(土壤中)에서 300여주(餘株)의 Lipase생산균(生産菌)을 분리(分離)하였으며 이들의 Lipase생산능(生産能)을 검토(檢討)하여 유용균주(有用菌株) 1주(株)를 선정(選定)하였다. (2) 선정(選定)된 균주(菌株)의 형태학적(形態學的) 및 생리학적성질(生理學的性質)을 검토(檢討)한바 Lodder manual 의 Trichosporon cutaneum에 속(屬)하는 균주(菌株)로 인정(認定)되었다.

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포도당에 의해 합성억제되는 알카리성 Lipase를 생성분비하는 Pseudomonas aeruginosa 균주의 분리 및 이 효소의 정제 (Isolation of a Pseudomonas aeruginosa Strain Producing an Extracellular Alkaline Lipase Catabolitely Regulated by Glucose, and Purification of the Lipase)

  • 이정미;김란숙;김병오;박영덕;진익렬
    • 한국미생물·생명공학회지
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    • 제21권3호
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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.

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Back-Extraction Processes of C.C.Lipase with Mediated AOT Reverse Micellar System

  • Lee, Sung-Sik;Kim, Bong-Gyu;Sung, Nak-Chang;Lee, Jong-Pal
    • Bulletin of the Korean Chemical Society
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    • 제25권6호
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    • pp.873-877
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    • 2004
  • The relationship between the behaviors of c.c.lipase back-extraction and their percolation phenomena by using AOT reverse micellar systems (RVMS) has been studied by the addition of a small amount of additives to organic phase such as thiols and nonionic-surfactants focusing on micelle-micelle interactions. The values of ${\beta}_t$ defined by the variation of percolation processes and back-extraction behaviors of c.c.lipase have a good linear correlation. The hydrophobicity of additive molecules suppressing the cluster formation of reverse micelles (high values of ${\beta}_t$) improved the back-extraction behavior of c.c.lipase. The back-extraction fraction and its rate of c.c.clipase are increased with decreasing of the value of hydrophilic lipophilic balance (HLB) and increasing of the hydrophobicity per additive molecules added to reverse micellar systems (RVSM) in the same additives concentration.

Effect of Enzymatic Hydrolysis on Polylactic Acid Fabrics by Lipases from Different Origins

  • Lee, So-Hee;Song, Wha-Soon
    • 한국의류학회지
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    • 제36권6호
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    • pp.653-662
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    • 2012
  • This study measured the effect of general pre-treatment on PLA fabrics to confirm the benefits of enzymatic processing on PLA fabrics in the textile industry as well as evaluated the hydrolytic activities of three lipases. The effects of lipase hydrolysis were analyzed through moisture regain, dyeing ability, tensile strength, and surface morphology. As a result, PLA fibers were easily damaged by a low concentration of sodium hydroxide and a low treatment temperature. The optimal treatment conditions of Lipase from Candida cylindracea were pH 8.0, $40^{\circ}C$, and 1,000 U. The optimal treatment conditions for Lipase from Candida rugosa were pH 7.2, $37^{\circ}C$, and 1,000 U. The optimal treatment conditions for Lipase from Porcine pancreas were pH 8.0, $37^{\circ}C$, and 2,000 U. The moisture regain and dyeing ability of PLA fabrics increased and the tensile strength of PLA fabrics decreased. The results of surface morphology revealed that there were some cracks due to hydrolysis on the surface of the fiber.

Purification and Characterization of the Lipase from Acinetobacter sp. B2

  • Sohn, Sung-Hwa;Park, Kyeong-Ryang
    • Molecular & Cellular Toxicology
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    • 제1권3호
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    • pp.189-195
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    • 2005
  • Industrial development has increase consumption of crude oil and environmental pollution. A large number of microbial lipolytic enzymes have been identified and characterized to date. To development for a new lipase with catalytic activity in degradation of crude oil as a microbial enzyme, Acinetobactor sp. B2 was isolated from soil samples that were contaminated with oil in Daejon area. Acinetobactor sp. B2 showed high resistance up to 10 mg/mL unit to heavy metals such as Ba, Li, Al, Cr, Pb and Mn. Optimal growth condition of Acinetobactor sp. B2 was confirmed $30^{\circ}C$. Lipase was purified from the supernatant by Acinetobactor sp. B2. Its molecular mass was determined to the 60 kDa and the optimal activity was shown at $40^{\circ}C$ and pH 10. The activation energies for the hydrolysis of p-nitrophenyl palmitate were determined to be 2.7 kcal/mol in the temperature range 4 to $37^{\circ}C$. The enzyme was unstable at temperatures higher than $60^{\circ}C$. The Michaelis constant $(K_{m})\;and\;V_{max}$ for p-nitrophenyl palmitate were $21.8{\mu}M\;and\;270.3{\mu}M\;min^{-1}mg\;of\;protein^{-1}$, respectively. The enzyme was strongly inhibited by $Cd{2+},\;Co^{2+},\;Fe^{2+},\;Hg^{2+},\;EDTA$, 2-Mercaptoethalol. From these results, we suggested that lipase purified from Acinetobactor sp. B2 should be able to be used as a new enzyme for degradation of crude oil, one of the environmental contaminants.

부처손(Selaginella tamariscina) 추출물의 리파아제 저해 활성 및 지질 축적 억제 효과 (The Effect of Selaginella tamariscina on Inhibition of Pancreatic Lipase and Lipid Accumulation)

  • 김건희;이신영;이애랑
    • 한국식품영양학회지
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    • 제32권1호
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    • pp.27-32
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    • 2019
  • The objective of this study was to evaluate novel usability as natural anti-obesity supplement of Selaginella tamariscina extract. The total phenol contents and total flavonoid contents were $60.29{\pm}3.11GAE\;mg/g$ and $14.90{\pm}0.34QE\;mg/g$, respectively. To evaluate anti-obesity activity of Selaginella tamariscina extract, pancreatic lipase inhibition activity as well as its inhibition effect of lipid accumulation in adipocytes were conducted by Oil Red O staining and lipolysis assay. The result of pancreatic lipase inhibition activity of S. tamariscina extract showed a wide range between 40 and 73% dose dependently. While the incubation of 3T3-L1 cells with S. tamariscina extract inhibited differentiation of preadipocytes and reduced lipid accumulation, the level of released free glycerol into culturing medium was increased in multiple concentrations. These results showed that S. tamariscina extract inhibit adipogenesis and pancreatic lipase activity. Thus, S. tamariscina extract can be a candidate for regulating lipid accumulation in obesity.