• 제목/요약/키워드: Lipase stability

검색결과 59건 처리시간 0.031초

Studies on the Inhibitory Effect of Eugenia aromaticum Extract on Pancreatic Lipase

  • Kim, Seung-Kyum;Kim, Yong-Mu;Hong, Mi-Jeong;Rhee, Hae-Ik
    • Journal of Applied Biological Chemistry
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    • 제48권2호
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    • pp.84-88
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    • 2005
  • To develop functional food and anti-obesity drug through inhibition of dietary lipid absorption, inhibitory effects of herb extracts on pancreatic lipase were investigated. Due to high yield and simplicity of isolation, lipase inhibitor (ELI) was isolated from ethyl acetate extract of Eugenia aromaticum, which showed highest inhibitory activity, and characterized for development of novel functional material. Stability of ELI at high temperature and low pH was investigated. Results showed ELI is relatively stable under thermal and acidic conditions, reversible, and noncompetitive inhibitor of pancreatic lipase.

Biodiesel Production Using a Mixture of Immobilized Rhizopus oryzae and Candida rugosa Lipases

  • Lee, Dong-Hwan;Kim, Jung-Mo;Shin, Hyun-Yong;Kang, Seong-Woo;Kim, Seung-Wook
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제11권6호
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    • pp.522-525
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    • 2006
  • Biodiesel conversion from soybean oil reached a maximum of 70% at 18 h using immobilized 1,3-specific Rhizopus oryzae lipase alone. Biodiesel conversion failed to reach 20% after 30 h when immobilized nonspecific Candida rugosa lipase alone was used. To increase the biodiesel production yield, a mixture of immobilized 1,3-specific R. oryzae lipase and nonspecific C. rugosa lipase was used. Using this mixture a conversion of greater than 99% at 21 h was attained. When the stability of the immobilized lipases mixture was tested, biodiesel conversion was maintained at over 80% of its original conversion after 10 cycles.

감태 추출물이 지니는 Lipase 저해활성의 열 및 pH 안정성 (Inhibitory Effect of Ecklonia cava Extracts against Lipase Activity and Stability Effect of Temperature and pH on Their Activity)

  • 정지연;김꽃봉우리;이청조;곽지희;김민지;김동현;선우찬;김태완;안동현
    • 한국식품영양과학회지
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    • 제40권7호
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    • pp.969-974
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    • 2011
  • 본 연구는 감태 추출물의 lipase 저해활성을 알아보고, 산업적으로 이용가능성을 확인하기 위해 열 및 pH에 대한 안정성을 실시하였다. 감태의 일반성분을 측정한 결과, 수분함량은 8.1%, 회분함량은 26.5%, 조지방 함량은 1.2%, 조단백 함량은 12.9%, 탄수화물의 함량은 51.4%로 나타났다. 감태 추출물의 색도 및 pH를 측정한 결과, 에탄올 추출물이 물 추출물에 비해 명도 및 황색도가 높고 적색도는 낮은 것으로 나타났으며, 에탄올 추출물과 물 추출물이 산성과 약산성을 띠는 것으로 나타났다. 감태 추출물을 5, 2.5 및 1 mg/mL의 농도로 lipase 저해활성을 측정한 결과, 에탄올 추출물에서는 59, 34 및 19%의 저해활성을 보여 물 추출물보다 높은 저해활성을 보였다. 높은 저해활성을 보인 감태 에탄올 추출물의 열 및 pH에 대한 안정성을 측정한 결과, $100^{\circ}C$에서 20분, $121^{\circ}C$에서 15분의 열처리에 의해 lipase 저해활성이 증가하는 것으로 나타났으며, pH 2~10의 모든 범위에서도 안정한 것을 확인할 수 있었다. 이상의 결과를 통해 lipase 저해활성을 지니는 감태 에탄올 추출물이 열 및 pH에 대해 높은 안정성을 가져 항비만 소재로 응용할 수 있을 것으로 사료된다.

Pseudomonas sp. BCNU 154 유래의 유기용매 내성 리파아제 (Organic Solvent-tolerant Lipase from Pseudomonas sp. BCNU 154)

  • 최혜정;황민정;서정윤;주우홍
    • 생명과학회지
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    • 제23권10호
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    • pp.1246-1251
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    • 2013
  • 산업공단지역의 폐수에서 분리한 유기용매 내성 Pseudomonas sp. BCNU 154 리파아제의 최적조건은 $37^{\circ}C$, pH8로 조사되었다. BCNU 154의 crude 리파아제는 toluene에서 2시간 반응시 효소활성 약 6.01 U/ml (117.53%)로 가장 안정한 것으로 나타났다. 한편 $Ca^{2+}$, $Mg^{2+}$, $NH_4{^+}$, $Na^+$ 이온 및 triton X-100은 효소를 활성화시킨 반면에 $Ba^{2+}$, $Hg^{2+}$$Zn^{2+}$ 이온은 효소활성을 억제하였다. Pseudomonas sp. BCNU 154 리파아제는 상용 고정화 효소인 Novozym 435와 비교해서도 안정한 활성을 보였다. 그러므로 유기용매 내성 리파아제는 별도의 고정화 처리없이도 화학산업공정에서 가능성 있는 whole cell 생물촉매로서 유용할 것으로 판단된다.

Lipase의 Transesterification반응에 의한 생물계면활성제의 합성

  • 신영민;정숙현;이상옥;신화경;이희정;이태호
    • 한국미생물·생명공학회지
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    • 제25권4호
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    • pp.420-426
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    • 1997
  • Pseudomonas sp. lipase (lipase AK) catalyzed transesterification reaction between fructose and vinyl laurate in anhydrous pyridine. The product of this process was identified as monoester of fructose and vinyl laurate. The synthetic product has been found to be an excellent emulsifier. The synthetic bioemulsifier showed a good emulsification activity and stability in comparison with other commercial emulsifiers, and good emulsification activity on various emulsifying substrates.

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Optimization of Medium for Lipase Production from Zygosaccharomyces mellis SG1.2 Using Statistical Experiment Design

  • Pramitasari, Marisa Dian;Ilmi, Miftahul
    • 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.

Effects of Stirring and Addition of Chemical Compounds on Glycerolysis of Triglyceride in Reversed Micelles

  • Chang, Pahn-Shick
    • Journal of Microbiology and Biotechnology
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    • 제1권3호
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    • pp.197-201
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    • 1991
  • Glycerolysis of triolein by lipase from Chromobacterium viscosum lipase was studied batchwise in AOT-isooctane reversed micelles. The reaction mixture was extracted with chloroform and the content of triolein, 1, 2-diolein, 1, 3-diolein, 1-monoolein, and free fatty acid in the condensed chloroform solution was determined using high performance liquid chromatography (HPLC). The effect of agitation speed on the initial rate of conversion was examined. As the speed of agitation increased up to 700 rpm, the reaction rate increased. However, above 700 rpm, the rate approached maximum and did not increase that much. The glycerolysis activity and the stability of the enzyme were affected by stirring and addition of histidine or copper. Addition of histidine and copper increased the rates of glycerolysis but they are detrimental to the operational stability in reversed micelles.

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Analysis of the Structure-stability Relationship of Cold-adapted Lipase PsLip1 from Homology Modeling

  • Choo, Dong-Won
    • Genomics & Informatics
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    • 제9권2호
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    • pp.79-84
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    • 2011
  • Two initial models of cold-adapted lipase PsLip1 have been constructed, based on homology with the bacterial lipases Chromobacterium viscosum (CvLip) and Pseudomonas cepacia (PcLip), whose X-ray structures have been solved and refined to high resolution. The mature polypeptide chains of these lipases have 84% similarity. The models of Mod1 and Mod2 have been compared with the tertiary structures of CvLip and PcLip, respectively, and analyzed in terms of stabilizing interactions. Several structural aspects that are believed to contribute to protein stability have been compared: the number of conserved salt bridges, aromatic interactions, hydrogen bonds, helix capping, and disulfide bridges. The 3-dimensional structural model of PsLip1 has been constructed in order to elucidate the structural reasons for the decreased thermostability of the enzyme in comparison with its mesophilic counterparts.

Janthinobacterium sp. 유래 저온활성 lipase의 발현, 정제 및 효소 특성 연구 (Expression, Purification, and Characterization of a Cold-adapted Lipase from Janthinobacterium sp.)

  • 박성호;박성주;최종일
    • 한국미생물·생명공학회지
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    • 제46권1호
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    • pp.51-58
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    • 2018
  • 본 연구에서는 극지에서 유래한 Janthinobacterium sp. PAMC25641로부터 분리한 리파아제 유전자를 클로닝 하고 과발현시켜 정제하였으며, 이 분리한 재조합 리파아제 효소의 생화학적 특성에 대해 분석하였다. 이 효소는 $15^{\circ}C$ 이하의 온도에서 장시간 활성을 유지하는 효소로서 산업적으로 활용될 가능성이 높을 것으로 기대된다.

Role of Exopolymeric Substances (EPS) in the Stability of the Biofilm of Thiomonas arsenivorans Grown on a Porous Mineral Support

  • Michel, Caroline;Garrido, Francis;Roche, Emilie;Belval, Sylvain Challan;Dictor, Marie-Christine
    • Journal of Microbiology and Biotechnology
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    • 제21권2호
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    • pp.183-186
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    • 2011
  • Biochemical methods were selected to evaluate the role of exopolymeric substances in the stability of biofilms used in bioremediation processes. Biofilms of Thiomonas arsenivorans formed on pozzolana were thus treated with pronase (protein target), lectins (Con A or PNA), calcofluor or periodic acid (polysaccharides target), DNase (DNA target), and lipase (triglycerides target). Neither protease nor DNase treatments had any effect on bacterial adhesion. Lectins and calcofluor treatments mainly affected young biofilms. Lipase treatment had a noticeable effect on biofilm stability whatever the biofilm age. Results suggest that it would be an increased resistance of mature biofilms that protects them from external attacks.