Relevant bibliographies by topics / Lipase Lipase

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Academic literature on the topic 'Lipase Lipase'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Lipase Lipase"

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Bracco, Paula, Nelleke van Midden, Epifanía Arango, Guzman Torrelo, Valerio Ferrario, Lucia Gardossi, and Ulf Hanefeld. "Bacillus subtilis Lipase A—Lipase or Esterase?" Catalysts 10, no. 3 (March 7, 2020): 308. http://dx.doi.org/10.3390/catal10030308.

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The question of how to distinguish between lipases and esterases is about as old as the definition of the subclassification is. Many different criteria have been proposed to this end, all indicative but not decisive. Here, the activity of lipases in dry organic solvents as a criterion is probed on a minimal α/β hydrolase fold enzyme, the Bacillus subtilis lipase A (BSLA), and compared to Candida antarctica lipase B (CALB), a proven lipase. Both hydrolases show activity in dry solvents and this proves BSLA to be a lipase. Overall, this demonstrates the value of this additional parameter to distinguish between lipases and esterases. Lipases tend to be active in dry organic solvents, while esterases are not active under these circumstances.
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Sun, Jingjing, Yiling Chen, Jun Sheng, and Mi Sun. "Immobilization ofYarrowia lipolyticaLipase on Macroporous Resin Using Different Methods: Characterization of the Biocatalysts in Hydrolysis Reaction." BioMed Research International 2015 (2015): 1–7. http://dx.doi.org/10.1155/2015/139179.

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To improve the reusability and organic solvent tolerance of microbial lipase and expand the application of lipase (hydrolysis, esterification, and transesterification), we immobilized marine microbial lipase using different methods and determined the properties of immobilized lipases. Considering the activity and cost of immobilized lipase, the concentration of lipase was fixed at 2 mg/mL. The optimal temperature of immobilized lipases was 40°C and 5°C higher than free lipase. The activities of immobilized lipases were much higher than free lipase at alkaline pH (more than 50% at pH 12). The free lipase lost most activity (35.3%) and immobilized lipases retained more than 46.4% of their initial activity after 3 h heat treatment at 70°C. At alkaline pH, immobilized lipases were more stable than free lipase (more than 60% residue activity at pH 11 for 3 h). Immobilized lipases retained 80% of their activity after 5 cycles and increased enzyme activity (more than 108.7%) after 3 h treatment in tert-butanol. Immobilization of lipase which improved reusability of lipase and provided a chance to expand the application of marine microbial lipase in organic system expanded the application range of lipase to catalyze hydrolysis and esterification in harsh condition.
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Wang, Shang, Yan Xu, and Xiao-Wei Yu. "Micro-Aqueous Organic System: A Neglected Model in Computational Lipase Design?" Biomolecules 11, no. 6 (June 7, 2021): 848. http://dx.doi.org/10.3390/biom11060848.

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Water content is an important factor in lipase-catalyzed reactions in organic media but is frequently ignored in the study of lipases by molecular dynamics (MD) simulation. In this study, Candida antarctica lipase B, Candida rugosa lipase and Rhizopus chinensis lipase were used as research models to explore the mechanisms of lipase in micro-aqueous organic solvent (MAOS) media. MD simulations indicated that lipases in MAOS systems showed unique conformations distinguished from those seen in non-aqueous organic solvent systems. The position of water molecules aggregated on the protein surface in MAOS media is the major determinant of the unique conformations of lipases and particularly impacts the distribution of hydrophilic and hydrophobic amino acids on the lipase surface. Additionally, two maxima were observed in the water-lipase radial distribution function in MAOS systems, implying the formation of two water shells around lipase in these systems. The energy landscapes of lipases along solvent accessible areas of catalytic residues and the minimum energy path indicated the dynamic open states of lipases in MAOS systems differ from those in other solvent environments. This study confirmed the necessity of considering the influence of the microenvironment on MD simulations of lipase-catalyzed reactions in organic media.
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Guo, Chenchen, Rikuan Zheng, Ruining Cai, Chaomin Sun, and Shimei Wu. "Characterization of Two Unique Cold-Active Lipases Derived from a Novel Deep-Sea Cold Seep Bacterium." Microorganisms 9, no. 4 (April 10, 2021): 802. http://dx.doi.org/10.3390/microorganisms9040802.

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The deep ocean microbiota has unexplored potential to provide enzymes with unique characteristics. In order to obtain cold-active lipases, bacterial strains isolated from the sediment of the deep-sea cold seep were screened, and a novel strain gcc21 exhibited a high lipase catalytic activity, even at the low temperature of 4 °C. The strain gcc21 was identified and proposed to represent a new species of Pseudomonas according to its physiological, biochemical, and genomic characteristics; it was named Pseudomonas marinensis. Two novel encoding genes for cold-active lipases (Lipase 1 and Lipase 2) were identified in the genome of strain gcc21. Genes encoding Lipase 1 and Lipase 2 were respectively cloned and overexpressed in E. coli cells, and corresponding lipases were further purified and characterized. Both Lipase 1 and Lipase 2 showed an optimal catalytic temperature at 4 °C, which is much lower than those of most reported cold-active lipases, but the activity and stability of Lipase 2 were much higher than those of Lipase 1 under different tested pHs and temperatures. In addition, Lipase 2 was more stable than Lipase 1 when treated with different metal ions, detergents, potential inhibitors, and organic solvents. In a combination of mutation and activity assays, catalytic triads of Ser, Asp, and His in Lipase 1 and Lipase 2 were demonstrated to be essential for maintaining enzyme activity. Phylogenetic analysis showed that both Lipase 1 and Lipase 2 belonged to lipase family III. Overall, our results indicate that deep-sea cold seep is a rich source for novel bacterial species that produce potentially unique cold-active enzymes.
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Prasasty, Vivitri Dewi, Vinella Winata, and Muhammad Hanafi. "Identification and Characterization of Bacterial Lipase from Plateu Soil in West Java." Jurnal Kimia Terapan Indonesia 18, no. 02 (January 3, 2017): 103–8. http://dx.doi.org/10.14203/jkti.v18i02.85.

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Lipases are known as glycerol ester hydrolases that catalyze the hydrolysis of triglycerides into free fatty acids and glycerol. Lipases are found in human, animal, plant, and microorganisms. The aim of this research is to identify lipase producers and characterize bacterial lipase from West Java plateau soil. Plateau soil bacteria samples were isolated on lipase screening medium containing Rhodamine B. Olive oil was used as a substrate in screening and production medium bacterial lipases. From 16 bacterial isolate of lipase producers, 14 were identified as Bacillus sp. and the others were identified as Pseudomonas alcaligenes. All isolates were taken into production step to determine their lipase activities. Moreover, top 3 lipase activities out of 16 lipase activities were chosen to find the optimum pH and temperature. Both characterizations showed pH optimum and temperature optimum from each lipase. These optimum condition were used in heat stability characterization for each lipase samples. The result showed that lipase from isolate COK 2 in optimum pH 4 and temperature 50oC was the most stable lipase due to this sample has good and stable activity for 1 to 5 hours incubation time. Lipase sample from isolate COK 2 has good efficiency for lipase productivity in acid condition and high temperature. Results of this investigation could encourage utilization of these activity enhancers for various industrial applications.
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Palomo, Jose M., Claudia Ortiz, Manuel Fuentes, Gloria Fernandez-Lorente, Jose M. Guisan, and Roberto Fernandez-Lafuente. "Use of immobilized lipases for lipase purification via specific lipase–lipase interactions." Journal of Chromatography A 1038, no. 1-2 (June 2004): 267–73. http://dx.doi.org/10.1016/j.chroma.2004.03.058.

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Lestari, Puji, Santi Nur Handayani, and Oedjijono Oedjijono. "SIFAT-SIFAT BIOKIMIAWI EKSTRAK KASAR LIPASE EKSTRASELULER DARI BAKTERI Azospirillum sp. JG3." Molekul 4, no. 2 (November 1, 2009): 73. http://dx.doi.org/10.20884/1.jm.2009.4.2.65.

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Lipases are valuable biocatalysts because they act under extremely mild conditions, are stable in organic solvents, show broad substrate specificity and exhibit high stereoselectivity. Lipases play important role in various industries such as detergent, cosmetics, flavor, pharmacy and synthesis of organic compounds. The increasing of lipases requirements in industries is goading research to get new lipases resources commited. One of potential lipase resource is Azospirillum sp.JG3 bacteria from Microbiology Laboratory of Biology Faculty University of Jenderal Soedirman. The specific targets of this research are to get crude extract of lipase and investigate its biochemical characteristics. The method used were rejuvenation of Azospirillum sp.JG3 bacteria, inoculum production, determination of optimum production time and bacterium growth phase, extraction and production of lipase to get crude extract, and characterization the biochemical properties of lipase crude extract. The research resulted that crude extract of lipase from Azospirillum sp.JG3 had optimum temperature at 40 °C and optimum pH at pH 7. The lipase was a metalloenzyme with Ca2+ as its cofactor. The lipase was stable in three organic solvents tested, (chloroform, n-hexane and ether).
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Köffel, René, Rashi Tiwari, Laurent Falquet, and Roger Schneiter. "The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 Genes Encode a Novel Family of Membrane-Anchored Lipases That Are Required for Steryl Ester Hydrolysis." Molecular and Cellular Biology 25, no. 5 (March 1, 2005): 1655–68. http://dx.doi.org/10.1128/mcb.25.5.1655-1668.2005.

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ABSTRACT Sterol homeostasis in eukaryotic cells relies on the reciprocal interconversion of free sterols and steryl esters. The formation of steryl esters is well characterized, but the mechanisms that control steryl ester mobilization upon cellular demand are less well understood. We have identified a family of three lipases of Saccharomyces cerevisiae that are required for efficient steryl ester mobilization. These lipases, encoded by YLL012/YEH1, YLR020/YEH2, and TGL1, are paralogues of the mammalian acid lipase family, which is composed of the lysosomal acid lipase, the gastric lipase, and four novel as yet uncharacterized human open reading frames. Lipase triple-mutant yeast cells are completely blocked in steryl ester hydrolysis but do not affect the mobilization of triacylglycerols, indicating that the three lipases are required for steryl ester mobilization in vivo. Lipase single mutants mobilize steryl esters to various degrees, indicating partial functional redundancy of the three gene products. Lipase double-mutant cells in which the third lipase is expressed from the inducible GAL1 promoter have greatly reduced steady-state levels of steryl esters, indicating that overexpression of any of the three lipases is sufficient for steryl ester mobilization in vivo. The three yeast enzymes constitute a novel class of membrane-anchored lipases that differ in topology and subcellular localization.
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Araiza-Villanueva, M. G., D. R. Olicón-Hernández, J. P. Pardo, H. Vázquez-Meza, and G. Guerra-Sánchez. "Monitoring of the enzymatic activity of intracellular lipases of Ustilago maydis expressed during the growth under nitrogen limitation and its correlation in lipolytic reactions." Grasas y Aceites 70, no. 4 (July 19, 2019): 327. http://dx.doi.org/10.3989/gya.1049182.

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Under nitrogen starvation, Ustilago maydis forms lipid droplets (LDs). Although the dynamics of these organelles are known in the literature, the identity of the lipases implicated in their degradation is unknown. We determined lipase activity and identified the intracellular lipases expressed during growth under nitrogen starvation and YPD media by zymograms. The results showed that cytosolic extracts exhibited higher lipase activity when cells were grown in YPD. Under nitrogen starvation, lipase activity was not detected after 24 h of culture, resulting in lipid accumulation in LDs. This suggests that these lipases could be implicated in LD degradation. In the zymogram, two bands, one of 25 and the other of 37 kDa, presented lipase activity. The YPD extracts showed lipase activity in olive and almond oils, which contain triacylglycerols with mono and polyunsaturated fatty acids. This is the first report about U. maydis cytosolic lipases involved in LD degradation.
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Liu, Shao Quan, Huey Yie Lee, Bin Yu, Philip Curran, and Jingcan Sun. "Bioproduction of Natural Isoamyl Esters from Coconut Cream as Catalysed by Lipases." Journal of Food Research 2, no. 2 (March 29, 2013): 157. http://dx.doi.org/10.5539/jfr.v2n2p157.

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<p>This study investigated the bioproduction of isoamyl esters in coconut cream by lipases. Five lipases (palatase 20000 L, lipase AYS “Amano”, lipase A “Amano” 12, piccantase A and piccantase AN) were used to biosynthesize isoamyl esters in coconut cream supplemented with isoamyl alcohol. The lipases have different abilities to synthesize isoamyl esters with lipase AYS “Amano”, palatase 20000 L and piccantase A showing the highest potential. Bioproduction of isoamyl octanoate by palatase 20000 L was further examined under different conditions of temperature, pH, isoamyl alcohol concentration and lipase amount. Biosynthesis of isoamyl octanoate by palatase was not significantly affected at 30-50°C or pH of 4 to 7 and its maximum bioproduction was obtained at isoamyl alcohol concentration of 4% (v/v) and lipase amount of 6 mg 100 mL<sup>-1</sup> reaction mixture. The lipase-treated coconut cream may serve as a bioflavouring ingredient for food applications or for extraction of pure aroma chemicals.</p>
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Dissertations / Theses on the topic "Lipase Lipase"

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Sias, Barbara. "Etude de deux lipases apparentées aux lipases pancréatiques : lipase pancréatique humaine apparentée de type 2 et la lipase du plasma seminal caprin." Aix-Marseille 2, 2005. http://www.theses.fr/2005AIX22003.

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El, Kouhen Karim. "Identification et caractérisation d'une lipase chez Arabidopsis thaliana." Aix-Marseille 2, 2005. http://theses.univ-amu.fr.lama.univ-amu.fr/2005AIX22046.pdf.

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Dridi, Kaouther. "Evolution moléculaire et structurale des membres de la famille génique des lipases pancréatique." Thesis, Aix-Marseille, 2013. http://www.theses.fr/2013AIXM4019.

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Helicoverpa armigera et Epiphyas postvittana, deux insectes nuisibles pour l'agriculture, ont développé des résistances contre la plupart des insecticides connus. Les lipides étant les constituants majeurs de leur régime alimentaire, les fonctions digestives des lipases deviennent alors une cible privilégiée pour l'élaboration de nouveaux insecticides. L'identification récente de gènes codant pour l'expression de protéines potentiellement actives et inactives apparentées aux lipases pancréatiques (PLRP) dans le tractus digestif de ces deux insectes et dont le niveau de transcription varie en fonction de leur régime alimentaire a ouvert un nouveau champ de recherche. Dans le but de contribuer à cette thématique, nous avons construit cinq lipases recombinantes d'E. postvittana (EpLIPs) et testé leur expression dans trois systèmes différents (E.coli, P.pastoris et bacculovirus). Le tractus digestif de Helicoverpa armigera a été étudié par chromatographie échangeuse d'ions et les différentes protéines séparées ont été testées en spectrométrie de masse et sur pHstat pour l'activité. Les résultats obtenus ont permis de mettre en évidence, pour la première fois, la présence à la fois d'une lipase active et d'une lipase inactive dans le tractus digestif d'un lépidoptère. Par ailleurs, la caractérisation biochimique d'un mutant GPLRP2-Δ β9 a été faite dans le but de comprendre l'effet de cette boucle, partiellement délétée dans les lipases d'insectes, dans la spécificité du substrat. Nous avons pu montrer que cette boucle β9 est essentielle pour la stabilisation de la chaîne acyle durant la réaction de lipolyse
Helicoverpa armigera and Epiphyas postvittana, two major pest crops, have developed resistances against most of the known insecticides. Lipids being a major component of insect diet, digestive function of lipase are a target of choice for new insecticide design. The recent identification of active and inactive pancreatic lipase related protein (PLRP) genes in those two insects midgut, with a level of transcription depending on the diet, opened the field of insect digestive lipase study. In order to contribute to this thematic, we built five recombinants lipase from E. postvittana (EpLIPs) and tested their expression in three different systems (E.coli, P.pastoris and bacculovirus). Protein structure prediction of EpLIPs allowed us to develop some functional hypothesis enlightening the role of inactive lipase in lipid transport. H. armigera midgut contents were separated through a one step purification chromatography and the different fractions were tested for activity and mass spectrometry. The results obtained gave the first evidence of the presence of both an active and an inactive lipase in lepidopteran midgut. In addition to this work, a biochemical characterisation of a β9 GPLRP2 mutant was carried out to understand the effect of this loop, partially deleted in insect lipase, in substrate specificity. The result shows that β9 loop is essential for stabilizing the leaving acyl chain during the lipolysis reaction
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Qiu, Guosong. "Function of lipoprotein lipase and endothelial lipase in human macrophages." Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/31471.

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Lipoprotein lipase (LPL) and endothelial lipase (EL) are expressed in atherosclerotic lesions, mainly in macrophages. However, the functional roles of LPL and EL in macrophages are not well characterized. In the present thesis, the effects of these lipases on cholesterol efflux, low density lipoprotein (LDL) catabolism, and proinflammatory cytokine secretion in human macrophages were investigated. Lentivirus transduction successfully induced EL suppression or over-expression in macrophages. LPL suppression was mediated by lentivirus transduction whereas dexamethasone was used to stimulate LPL expression. Apolipoprotein AI- (apoAI-) mediated cholesterol efflux was modestly reduced after LPL and EL suppression, but significantly increased in lipase-overexpressing macrophages as well as transfected 293 cells. This effect was partially inhibited after the elimination of either catalytic or non-catalytic lipase function, but completely abolished when both functions were blocked. The observed effect on cholesterol efflux was mediated partially by an increased apoAI binding, an effect dependent on cell surface lipase. Lipase expression was inversely associated with phosphatidylcholine and sphingomyelin levels, but positively with lysophosphatidylcholine production, the later was shown to promote apoAI-mediated cholesterol efflux dose-dependently. EL expression was positively correlated with both native and oxidized LDL binding and association via non-catalytic function as observed in both EL-suppressed and over-expressed macrophages. By contrast, the catalytic activity of EL did not have a significant role in oxidized LDL metabolism with the exception of a positive correlation with native LDL association, which also partially depended on the LDL receptor. The concentration of interleukin-1β and 6, macrophage chemoattractant protein-1, and tumor necrosis factor-α was reduced after LPL and EL suppression, The lipase suppression also amplified the inhibitory effect of oxidized LDL in macrophages. Microarray analysis indicated that >50 genes, mainly proinflammatory ones, had marked expression changes after lipase suppression. Atorvastatin treatment reduced LPL and EL expression as well as Rho, the liver X receptor (LXR), and nuclear factor-κB (NF-κB) levels. Mechanistic studies identified LXR and NF-κB to be involved in atorvastatin-induced suppression of LPL and EL, respectively. In summary, by promoting apoAI-mediated cholesterol efflux, lipoprotein binding and uptake, and proinflammatory cytokine expression in macrophages, EL and LPL may influence the atherogenic potential of macrophages.
Medicine, Faculty of
Pathology and Laboratory Medicine, Department of
Graduate
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Fernandez, Sylvie. "Lipolyse d'excipients lipidiques destinés à l'administration par voie orale de substances actives hydrophobes." Aix-Marseille 2, 2008. http://theses.univ-amu.fr.lama.univ-amu.fr/2008AIX22024.pdf.

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Le Labrasol® et le Gelucire® 44/14 sont des macrogolglycérides utilisés pour l’administration par voie orale des substances actives hydrophobes. Ils sont composés d’acylglycérols et d’esters de PEG, substrats potentiels des lipases digestives. Nous avons étudié la lipolyse in vitro de ces excipients par les lipases digestives. Nous avons mis en évidence que la lipase pancréatique humaine (HPL), principale lipase impliquée dans la lipolyse des triacylglycérols alimentaires, n’était pas capable d’hydrolyser ces excipients contrairement à la lipase gastrique de chien (DGL), la lipase pancréatique apparentée de type 2 (HPLRP2) et la carboxyl ester hydrolase (CEH). L’étude de la spécificité des lipases digestives vis-à-vis des différents substrats contenus dans ces excipients montre que les esters de PEG sont de mauvais substrats pour la HPL et la DGL présentant une spécificité marquée pour les di- et triacylglycérols. En revanche, la HPLRP2 et la CEH hydrolysent les esters de PEG et ne sont pas spécifiques vis-à-vis des différents composés contenus dans ces excipients. Nous avons développé une méthode de simulation in vitro de la lipolyse gastro-intestinale de ces excipients prenant en compte la lipolyse gastrique puis la lipolyse duodénale. La composition des excipients lipidiques est significativement modifiée à la fin de la phase gastrique montrant l’importance de la lipolyse gastrique in vivo. Nous avons aussi étudié l’influence de la lipolyse gastro-intestinale du Labrasol® et du Gelucire® 44/14 sur la solubilité apparente de deux substances actives hydrophobes, le piroxicam et la cinnarizine. Il apparaît que la lipolyse gastro-intestinale de l’excipient n’entraîne pas de précipitation du piroxicam et permet de maintenir la cinnarizine en solution aqueuse lorsque celle-ci formulée avec le Labrasol®
Labrasol® and Gelucire® 44/14 are macrogolglycerides which are used for the oral drug delivery of poorly water-soluble drugs. They are composed of acylglycerols and PEG esters potential substrates of digestive lipases. We studied the in vitro lipolysis of these excipients by digestive lipases. We showed that the human pancreatic lipase (HPL), the main lipase involved in the lipolysis of dietary triacylglycerols, was not able to hydrolyze either of these excipients contrary to dog gastric lipase (DGL), human pancreatic lipase-related protein 2 (HPLRP2), and carboxyl ester hydrolase (CEH). The study of digestive lipases specificity showed that HPL and DGL possessed specificity toward di- and triacylglycerols, whereas HPLRP2 and CEH hydrolyzed PEG esters but did not present a marked specificity. We developed an in vitro method to simulate the gastrointestinal lipolysis of these excipients. At the end of the gastric phase, the composition of both of these excipients was significantly modified underlining the importance of gastric lipolysis in vivo. We also studied the influence of excipients’ lipolysis on the concentration of two poorly water-soluble drugs, piroxicam and cinnarizine, in the aqueous phase. It seems that the gastrointestinal lipolysis of these excipients did not undergo piroxicam precipitation whereas it was a prerequisite to maintain cinnarizine in aqueous solution when formulated with Labrasol®
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Infanzón, Ramos Belén. "Novel Lipases: Expression and Improvement for Applied Biocatalysis = Nuevas lipasas: expresión y mejoras para biocatálisis aplicada." Doctoral thesis, Universitat de Barcelona, 2017. http://hdl.handle.net/10803/456674.

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This thesis is focused in the identification and improvement of lipases for biotechnological application. The importance of lipases is increasing in several industries. However, the commercial use of lipases is still a drawback in the economics of the lipase-based industrial applications. There are many tools for improving and adapting the enzyme properties to the desired requirements of a process that could lead lipase catalysis through a cost-effective process. In this context, the main objective of this work was: “To characterize, express and to improve novel bacterial lipases for sustainable industrial processes”. The first activity done was to explore and to characterize a new esterase from P. barcinonensis. It was isolate from P. barcinonensis the gene corresponding to Est23, and its cloning in a proper vector to perform expression and purification for biochemical characterization. Est23 showed preference for mid-chain substrates and having maximum activity at 37 °C and pH 7. It also includes in silico analysis of the 3D model structure and phylogeny. Moreover, a phylogenetic tree was constructed to assign Est23 to one of the bacterial hydrolase families described by Arpingy and Jaeger. Est23 could not be assigned to any bacterial hydrolases described till that moment, suggesting that Est23 could be part of a new group of bacterial lipases. Because Est23 displays a GGG(A)X-type putative oxyanion hole, widely described as a motif involved in tertiary alcohol resolution, the ability of Est23 for conversion and resolution of tertiary alcohols was evaluated. However, no conversion was detected using the esters linalyl and terpinyl acetate alcohols as substrates. To improve LipR activity by protein engineering LipR was then desired. LipR was isolated from Rhodococcus sp. strain CR-53 in a previous and showed an unusual fungal-like oxyanion-hole never found among bacterial lipases, close to the Y-type oxyanion hole described for Candida antartica lipase A (CalA), a lipase widely used in industry. In order to improve LipR activity on long-chain substrates, several enzyme-engineering approaches were done to change the amino acids constituting the rare oxyanion hole of LipR for further industrial application. These mutations also allowed studying the role of the amino acids forming the oxyanion hole of LipR. Hydrolytic activity over short, mid and long- chain substrates was assayed with the variants obtained. The LipR variant Asp111Gly produced a change on the chain- length- substrate preference of LipR, displaying a 5.6 fold increase of activity on muf-oleate. This improvement of activity on longer chain length substrates makes of this LipR variant a very attractive candidate for testing activity on biodiesel synthesis, a process requiring activity on long-chain substrates. Nevertheless, LipR and LipR_YGS variant need a clear expression enhancement in order to apply them to transesterification reactions using oily feedstocks. The stabilization Pseudomonas lipases LipA, LipC and LipCmut was improved by immobilization in order to applied these enzymes in transesterification reactions. Therefore, a fast and economic immobilization procedure by adsorption was set up. Finally, the three immobilized lipase preparations and a commercial lipase were used to test alternative feedstocks for triglyceride transesterification. A total of four oils were tested: commercial triolein, degummed soybean oil, waste cooking oil, and Mucor circinelloides oil. Moreover, the characterization of the tested raw materials in terms of FFAs, tri, di and monoglyceride contents measure was also of interest. In a global analysis, a good increase of FAMEs percent was obtained with LipA, LipC and LipCmut immobilized on Accurel MP1000. But better results were achieved when the reactions were catalyzed by Novozym® 435 commercial enzyme.
Esta tesis se centra en la identificación y mejora de lipasas para aplicaciones biotecnológicas. El objetivo principal de este trabajo fue: "Caracterizar, expresar y mejorar las nuevas lipasas bacterianas para procesos industriales sostenibles". La primera actividad realizada fue explorar y caracterizar una nueva esterasa, Est23, de P. barcinonensis. Se aisló de P. barcinonensis el gen correspondiente a Est23 y su clonación en un vector adecuado para realizar la expresión y purificación para caracterización bioquímica. Además, se construyó un árbol filogenético para asignar Est23 a una de las familias de hidrolasas bacterianas descritas por Arpingy y Jaeger, y debido a que Est23 tiene un oxyanion-hole de tipo GGG (A) X, ampliamente descrito como motivo implicado en la resolución del alcohol terciario, se evaluó la capacidad de Est23 en dichas reacciones. Luego se buscó mejorar la actividad sobre sustratos de cadena larga de la lipasa LipR de Rhodococcus sp. por ingeniería de proteínas. Diferentes enfoques de ingeniería enzimática se realizaron para cambiar los aminoácidos que forman parte del atípico oxyanion-hole de LipR. Estas mutaciones también permitieron estudiar el papel de los aminoácidos que forman este motivo. La actividad hidrolítica de las variantes obtenidas fue ensayada sobre sustratos de cadena corta, media y larga. La variante LipR Asp111Gly produjo un cambio en la preferencia de LipR de longitud de cadena. Sin embargo, LipR y LipR_YGS necesitan un aumento de expresión para aplicarlos a reacciones de transesterificación. La estabilización de tres lipasas de Pseudomonas, LipA, LipC y LipCmut, se mejoró por inmovilización con el fin de aplicar estas enzimas en las reacciones de transesterificación. Por lo tanto, se estableció un procedimiento de inmovilización por adsorción rápido y económico. Finalmente, se usaron las tres lipasa inmovilizadas y una lipasa comercial para probar materias primas alternativas para la transesterificación de triglicéridos. Se probaron un total de cuatro aceites: trioleína comercial, aceite de soja desgomado, aceite de cocina de desecho y aceite de Mucor circinelloides. Además se realizó la caracterización de las materias primas ensayadas en términos de la medida de los ácidos grasos, tri, di y monoglicéridos.
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Frenken, Leo G. "Pseudomonas glumae lipase : characterization, biogenese and protein engineering = Pseudomona glumae lipase /." [S.l. : s.n.], 1993. http://www.gbv.de/dms/bs/toc/131132261.pdf.

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Allouche, Maya. "Etude des interactions protéine-lipide : exemple du système lipase/colipase pancréatique." Aix-Marseille 2, 2008. http://www.theses.fr/2008AIX20674.

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Büchner, Susanne. "Bestimmung mikrobieller und gewebseigener Lipasen mit dem Reflectoquant® Lipase – Test (Merck KGaA)." Doctoral thesis, Universitätsbibliothek Leipzig, 2007. http://nbn-resolving.de/urn:nbn:de:bsz:15-20071024-093300-7.

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Fetthaltige Lebensmittel tierischer Herkunft sind aufgrund ihres hohen Lipidgehaltes besonders anfällig für Lipolyse. Ausschlaggebend hierfür ist die Wirkung mikrobieller und gewebseigener Lipasen. Für die Beurteilung der Haltbarkeit und Qualität derartiger Lebens-mittel werden vorwiegend die sensorische Prüfung und mikrobiologische Untersuchungen eingesetzt. Eine Einschätzung lipolytischer Aktivitäten erfolgt derzeit nicht routinemäßig. Von Seiten der Lebensmittelindustrie und der Lebensmittelüberwachung besteht, besonders im Zusammenhang mit Qualitätssicherungssystemen, großes Interesse an einer schnellen Verfügbarkeit von Ergebnissen, um das Verderbnispotential der Lebensmittel effizienter abschätzen zu können. Schwerpunkte dieser Arbeit bildeten daher:  die Entwicklung von Applikationsvorschriften zur Bestimmung bakterieller und gewebs-eigener Lipasen mit dem Reflectoquant ® Lipase – Test, einem für Milchlipasen konzi-pierten Schnelltest der Fa. Merck,  die Messung synthetisierter Lipasekonzentrationen ausgewählter Verderbniserreger (n= 168) bzw. gewebseigener Lipasen (n= 127) in Fleisch (Schwein, Rind, Hähnchen, Kaninchen), Fisch (Kabeljau, Forelle, Hering), Wurst- und Fischerzeugnissen sowie Leber (Schwein, Pute),  die Erfassung von Konzentrationen nach 5-minütiger Erhitzung bei 50, 60, 70 und 80 °C, um eventuelle Unterschiede in der Thermoresistenz von bakteriellen und gewebseigenen Lipasen aufzuzeigen sowie  der Vergleich der Substratverwertbarkeit verschiedener bakterieller Lipasen gegenüber Caprylat, Tributyrin und Tween 60. Folgende Ergebnisse wurden erzielt:  Der Anwendungsbereich des Reflectoquant ® Lipase – Tests konnte um 5 Applikations-vorschriften zur Messung bakterieller Lipasekonzentrationen in Nährbouillon und zur Messung gewebseigener Lipasekonzentrationen in den oben aufgeführten Produkten erweitert werden. Dabei wurden Lösungsvorschläge zur Beseitigung von Störeinflüssen wie z.B. Ascorbinsäure in Wursterzeugnissen, erarbeitet.  Unter Verwendung des Reflectoquant ® Lipase – Tests konnte das lipolytische Synthesepotential von 56 Bakterienstämmen der Spezies Ps. aeruginosa, Ps. fluorescens, A. hydrophila, A. caviae, S. aureus, S. epidermidis, B. subtilis, P. mirabilis und Ser. marcescens nach Anzüchtung unter Optimalbedingungen bestimmt werden. Als besonders starke Lipasebildner mit Konzentrationen von > 50 µg/l, fielen Stämme von Ps. aeruginosa, Ps. fluorescens, A. hydrophila und S. aureus auf.  Für die Lebensmittel Fleisch, Fisch und Leber wurden erstmals Orientierungswerte zu natürlich enthaltenen Lipasekonzentrationen (gewebseigene Lipasen) ermittelt. Die Lipasekonzentrationen in Fleisch bewegten sich zwischen 44 µg/kg (Schwein) und 370 µg/kg (Kaninchen). In Fisch lagen sie zwischen 228 µg/kg (Kabeljau) und 1200 µg/kg (Forelle). Die höchsten Konzentrationen wurden in Schweineleber mit 122100 µg/kg gemessen.  Die nach Erhitzung gemessenen Konzentrationen bestätigen, dass bakterielle Lipasen wesentlich hitzestabiler sind als gewebseigene. Besonders hitzestabile Lipasen mit Restaktivitäten zwischen 16 % und 31 % nach 5-minütiger Erhitzung bei 70 °C bildeten die Stämme Ps. aeruginosa 5x und 1, Ps. fluorescens 9 und S. aureus 4.  Die geringe Hitzestabilität der gewebseigenen Lipasen (keine Restaktivitäten in Fisch, Rind-, Schweine- und Geflügelfleisch nach 5 min bei 70 °C) ist die Ursache für den fehlenden Lipasenachweis in den geprüften Brüh- und Kochwürsten (z.B. Bierschinken). Aufgrund dieser Unterschiede ist eine Abgrenzung bakterieller von gewebseigenen Lipasen möglich. Nachgewiesene Lipasekonzentrationen in erhitzten Produkten könnten daher ein Hinweis auf einen hohen Ausgangskeimgehalt mit Lipasesynthese und/oder mangelnde Erhitzung sein. Zu berücksichtigen ist allerdings, dass in lipasereichen Geweben, z.B. Leber, noch sehr geringe Lipasekonzentrationen nach Erhitzung auf 70 °C nachweisbar waren.  Von den drei Substraten wurden besonders gut Tributyrin und Caprylat von den getesteten bakteriellen Lipasen hydrolysiert. Die Prüfung der Substratverwertbarkeit hat insbesondere Bedeutung für die Einschätzung der Wirkung von Lipasen und die Voraussage der Haltbarkeit fetthaltiger Lebensmittel. Mit der nunmehr breiteren Anwendung des Reflectoquant ® Lipase – Tests und den neugewonnenen Kenntnissen über Lipasekonzentrationen in Lebensmitteln könnte möglicherweise, unter Einbeziehung der Gesamtkeimzahlbestimmung und sensorischen Eindrücken, die Einschätzung des Verderbs bzw. der Haltbarkeit präzisiert werden. Welche konkreten Lipasekonzentrationen lebensmittelhygienisch in Bezug auf Haltbarkeit und Qualität relevant sind, muss für die einzelnen Lebensmittel in Lagerungsversuchen und begleitenden mikrobiologischen Untersuchungen noch geprüft werden.
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Wannerberger, Kristin. "Lipases at solid surfaces an adsorption and activity study /." [Lund : Dept. of Food Technology, Lund University], 1996. http://catalog.hathitrust.org/api/volumes/oclc/38950353.html.

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Books on the topic "Lipase Lipase"

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Doolittle, Mark, and Karen Reue. Lipase and Phospholipase Protocols. New Jersey: Humana Press, 1998. http://dx.doi.org/10.1385/1592595812.

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Mala, J. Geraldine Sandana. Perspectives on lipase enzyme technology. Hauppauge, N.Y: Nova Science Publishers, 2009.

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Satoru, Takeuchi, ed. Perspectives on lipase enzyme technology. Hauppauge, N.Y: Nova Science Publishers, 2009.

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Mala, J. Geraldine Sandana. Perspectives on lipase enzyme technology. New York: Nova Science Publishers, 2009.

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Rees, Gareth David. Lipase catalysis in microemulsion-based systems. Norwich: University of East Anglia, 1990.

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Hendriks, Wilhelmina Leonie. Lipoprotein lipase-mediated interactions of lipoproteins with macrophages. [Leiden: University of Leiden, 1998.

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Ravindra, Pogaku, and Kenthorai Raman Jegannathan. Production of biodiesel using lipase encapsulated in κ-carrageenan. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-10822-3.

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Jenta, Tuah R. J. Catalytic studies of lipase in microemulsion-based reaction media. Norwich: University of East Anglia, 1993.

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Kontkanen, Hanna. Novel steryl esterases as biotechnological tools. [Espoo, Finland]: VTT Technical Research Centre of Finland, 2006.

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Chang, Shau-Feng. Studies on structure, heparin-binding, and gene expression of hepatic lipase. München: Dissertationsverlag NG Kopierladen, 1993.

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Book chapters on the topic "Lipase Lipase"

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Konwar, B. K., and Kalpana Sagar. "Introduction." In Lipase, 1–23. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-1.

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Konwar, B. K., and Kalpana Sagar. "Genomic Study of Culturable Bacteria." In Lipase, 163–92. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-10.

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Konwar, B. K., and Kalpana Sagar. "Microbial Assay of Culture Supernatant Containing Crude Lipase." In Lipase, 193–99. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-11.

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Konwar, B. K., and Kalpana Sagar. "Critical Observations." In Lipase, 201–5. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-12.

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Konwar, B. K., and Kalpana Sagar. "Application of Lipases." In Lipase, 25–34. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-2.

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Konwar, B. K., and Kalpana Sagar. "Metagenomics and Unculturable Bacteria." In Lipase, 35–51. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-3.

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Konwar, B. K., and Kalpana Sagar. "Accessing Metagenomics." In Lipase, 53–59. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-4.

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Konwar, B. K., and Kalpana Sagar. "Metagenomics for Lipase." In Lipase, 61–96. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-5.

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Konwar, B. K., and Kalpana Sagar. "Functional Approach for Metagenomic Library Construction." In Lipase, 97–110. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-6.

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Konwar, B. K., and Kalpana Sagar. "Overexpression of Recombinant Protein." In Lipase, 111–25. Toronto ; New Jersey : Apple Academic Press, 2018.: Apple Academic Press, 2018. http://dx.doi.org/10.1201/9781315159232-7.

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Conference papers on the topic "Lipase Lipase"

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K. Scherbakova, Valeria, and Alla A. Krasnoshtanova. "OBTAINING MICROPARTICLES OF CALCIUM CARBONATE LOADED WITH MICROBIAL LIPASE." In GEOLINKS International Conference. SAIMA Consult Ltd, 2020. http://dx.doi.org/10.32008/geolinks2020/b1/v2/09.

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At present, lipases of animal and microbial origin are increasingly used in human practice, namely in cheese production, milk chocolate production, confectionery industry, dry egg powder, production of flour, leather industry (for degreasing wool, bristles, leather), silk production, washing agents, as well as biodiesel. However, the practical use of lipase is limited by its low stability, reduced storage activity, and inability to reuse. One way to overcome these disadvantages is to microencapsulate the enzyme into various carriers. One promising carrier is calcium carbonate, characterized by ease of production and low cost. Therefore, the purpose of this work was to select the conditions for including lipase in the calcium carbonate microparticles. As the subject of the investigation, lipase of bacteria p. Pseudomonas fluorescens with activity of 27 u/mg was used in the work. This paper compares two methods of including protein molecules in carbonate microparticles: adsorption in pores (previously prepared carrier microparticles are added to the protein solution) and microencapsulation (formation of microparticles occurs simultaneously with inclusion of protein molecules). For both ways the capacity of microparticles of a carbonate of calcium by a bacterial lipase was determined and it was established that the maximum capacity equal was 0.2 mg/mg was reached when using a method of adsorption in pores. The specific activity of lipase in this case is 5.21 units/mg. The dynamics of bacterial lipase release from carbonate microparticles has been investigated. It has been found that within 90 minutes the degree of lipase release from microparticles does not exceed 28%, and the decrease in its specific activity does not exceed 10%. This fact suggests a higher prolongation of the action of lipase included in calcium carbonate microparticles compared to native. The operational stability of the bacterial lipase included in the calcium carbonate microparticles was evaluated as compared to native lipase. It was found that the temperature optimum did not occur, it remained at 37 ° C, but the operating stability increased in the lower temperature area. The optimum pH shifted from the slightly alkaline (pH 8.0) towards the neutral (pH 7.0), wherein in the region of alkaline pH values the operational stability of the microencapsulated lipase significantly increases. Microencapsulation of bacterial lipase into carbonate microparticles has been shown to increase storage stability by a factor of twice that of native.
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Bhushan, Indu. "Efficient media for high production of microbial lipase from Bacillus subtilis (BSK-L) using response surface methodology for enantiopure synthesis of drug molecules." In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.044.

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Lipases are a multipurpose enzyme that holds a significant position in industrial applications due to its ability to catalyse a large number of reactions such as hydrolysis, esterification, interesterification, transesterification which makes it a potential candidate. It is also used for the separation of chiral drugs from the racemic mixture and this property of lipase is considered very important in pharmaceutical industries for the synthesis of enantiopure bioactive molecules. Assuming the tremendous importance of lipases, as stereoselective biocatalysts, in pharmaceuticals and various other commercial applications, industrial enzymologists have been forced to search for those microorganisms which are able to produce novel biocatalysts at reasonably high yield. In the present study microbial lipase was isolated from the water sample of pond at Katra, Jammu and Kashmir (India). This enzyme has shown wide specificity and higher enantioselectivity, which make it pharmaceutical important enzyme. To make it economical for industrial application, it was produced on cheap nutrient media using Response Surface Methodology and got maximum production. It was used for resolution of chiral drugs and the significant results obtained during the course of work shall have potential towards pharmaceutical industries.
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Maggi, A., T. W. Barrowcliffe, E. Gray, M. B. Donati, R. E. Merton, and I. Pangrazzi. "RELATIONSHIP BETWEEN HAEMORRHAGIC AND LIPASE-RET EASING PROPERTIES OF HEPARIN AND LMV HEPARIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642929.

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In a preliminary study, a good correlation (r = 0.97) was noted between the relative abilities of an unfractionated heparin, a LMW heparin, pentosan poly sulphate and dermatan sulphate to prolong the template bleeding time in rabbits and their lipase-releasing potencies. In the present study, we have measured the prolongation of both the template and transection bleeding times in groups of 5 rats given i.v. injections of 0.75 mg/kg of two different unfractionated heparins (UEH), A and B, three different LMW heparins, X, Y and Z, and a heparan sulphate, HS. Lipase release was measured in plasma samples from different groups of 5 rats, using a tritiated triolein method.UFH A had the most haemorrhagic effect, with an approximate doubling of both template and transection bleeding times and was also the most potent lipase-releaser, giving an average lipase level of 1126 mu/ml. UFH B had no significant effect on the template bleeding time, but did prolong the transection time; its lipase releasing potency was 70% of UFH A. IMW heparin X had no effect on template or transection bleeding time and released only 40% lipase compared with UEH A. LMW heparins Y and Z did not affect the template bleeding time but did prolong the transection time; they released more lipase (60%) than LMW heparin X. Correlation coefficients with lipase release were 0.97 for the template bleeding time and 0.69 for the transection bleeding time. HS released only 7% lipase but gave significant prolongations of both bleeding times.These results confirm a strong positive correlation between the haemorrhagic and lipase releasing properties of heparin and LMW heparin, suggesting very similar structural requirements for the two biological activities. This correlation exists also for dermatan sulphate and pentosan polysulphate, but not for the heparan sulphate sample tested.
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Zhang, Lun, Wudi Zhang, Fang Yin, Xuerong Zhou, Jianchang Li, Rui Xu, Yubao Chen, and Shiqing Liu. "Lipase Catalyzed Production of Biodiesel." In 2010 Asia-Pacific Power and Energy Engineering Conference (APPEEC 2010). IEEE, 2010. http://dx.doi.org/10.1109/appeec.2010.5448148.

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Huang, Zhihong, Jing Gao, Tiantao Zhao, Weijie Li, Liya Zhou, and Ying He. "Lipase Catalyzed Synthesis of Ethyl Lactate." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE 2009). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5163016.

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Lopes Demito, Matheus, Luciano Fernandes, and Juliana Vitoria Messias Bittencourt. "Perspectivas Biotecnológicas da Produção de Lipase." In Simpósio de Bioquímica e Biotecnologia. Londrina - PR, Brazil: Galoa, 2017. http://dx.doi.org/10.17648/simbbtec-2017-80925.

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Oliveira, Wanderley Pereira, Tales Alexandre Costa-Silva, Ana Karine Furtado Carvalho, Claudia Regina Fernandes Souza, Larissa De Freitas, and Heizir F. Castro. "Immobilization of Candida rugosa lipase on eco-friendly supports by spouted-bed technology: Use in the synthesis of isoamyl caprylate." In 21st International Drying Symposium. Valencia: Universitat Politècnica València, 2018. http://dx.doi.org/10.4995/ids2018.2018.7544.

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Candida rugosa lipase (LCR) was immobilized on low-cost supports (by-products) and dried using a spouted-bed system. The yields of immobilized derivatives were in the range 61.5–78.7%. Lipase immobilized on rice husk showed the best results, presenting 94.1% of the original activity, followed by sugarcane bagasse (90.3%) and green coconut fiber (87.3%). Moisture content in the obtained powders varied between 4.7 and 5.6% and the water activities were in the range 0.21–0.35. Among all the tested biocatalysts for aroma production the lipase immobilized on rice husk showed the highest activity towards the formation of isoamyl caprylate (62.40 g.L-1). Keywords: Spouted bed dryer; Enzyme dehydration; Enzyme immobilization; Enzyme stabilization; Aroma production.
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Duarte, Amanda Alves, Renata Andrade De Oliveira, Eliane Pereira Cipolatti, Evelin Andrade Manoel, and Martina Costa Cerqueira. "COMPARAÇÃO DO DESEMPENHO DE LIPASE COMERCIAL E RECOMBINANTE DE CANDIDA ANTARCTICA FRAÇÃO B EM PARTÍCULAS DE PMMA." In I Congresso de Engenharia de Biotecnologia. Revista Multidisciplinar de Educação e Meio Ambiente, 2021. http://dx.doi.org/10.51189/rema/1356.

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Introdução: As lipases possuem alto poder catalítico, realizando diversos tipos de reações e por isso são conhecidas como excelentes alternativas nas indústrias têxtil, farmacêutica, alimentícia, biocombustíveis, entre outras. O processo de imobilização pode promover o aumento e a manutenção da estabilidade das enzimas e possibilitar o reuso desses biocatalisadores, diminuindo os custos do processo. Desta forma, têm se estudado cada vez mais o aperfeiçoamento dos processos de imobilização. A importância industrial da aplicação de lipases imobilizadas é notável, e o desenvolvimento de novos biocatalisadores poderá influenciar beneficamente no desenvolvimento e avanço da biocatálise. Objetivo: Comparar o desempenho de duas lipases: a lipase B de Candida antarctica comercial (CalB) e a sua análoga recombinante obtida por cultivo submerso (LipB) em partículas casca-núcleo de poli(metacrilato de metila) (PMMA/PMMA) em reações de hidrólise e esterificação. Material e Métodos: O suporte PMMA/PMMA foi inicialmente tratado com etanol e água destilada. Após, foi adicionado volume correspondente de uma solução de CalB ou LipB em solução tampão fosfato de sódio (5 mM, pH 7). A atividade do sobrenadante foi monitorada utilizando p-nitrofenil-laurato (p-NFL). A atividade hidrolítica foi medida no espectro utilizando como substrato p-NFL, com agitação suave e banho a 30ºC. A atividade de esterificação foi avaliada em ácido oleico e etanol (1:1) a 45ºC. Resultados: As enzimas foram imobilizadas com elevada porcentagem de imobilização, 95,92% para CalB e 96,2% para LipB em 4h. Na atividade hidrolítica os resultados foram CalB 53,84 e LipB 49,89 U/g biocat. Atividade de esterificação obtivemos para a CalB 519,61 e LipB 392,12 U/g biocat. Conclusão: O polímero núcleo-casca, poderá ser usado com sucesso para imobilização. O biocatalisador home-made em desenvolvimento apresentou muitas vantagens e tem seus destaque tanto para atividade enzimática quanto para aplicação em reações de esterificação comparada a CalB que é uma enzima comercial. Embora o trabalho ainda se encontre em desenvolvimento, os resultados são promissores e o biocatalisador obtido poderá ser usado em diversas áreas industriais.
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VILLEGAS, M. C., R. C. GIORDANO, and M. P. A. RIBEIRO. "SÍNTESE DE BIODIESEL ETANÓLICO UTILIZANDO LIPASE SOLÚVEL." In XXII Congresso Brasileiro de Engenharia Química. São Paulo: Editora Blucher, 2018. http://dx.doi.org/10.5151/cobeq2018-pt.0915.

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Xin, Jiaying, and Jiawen Jiang. "Lipase-Catalyzed Synthesis of S-Naproxenal oleins." In 2015 International Conference on Education, Management, Information and Medicine. Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/emim-15.2015.46.

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Reports on the topic "Lipase Lipase"

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Xiao, Shan, Wangang Zhang, and Dong U. Ahn. Changes of Hormone Sensitive Lipase, Adipose Tissue Triglyceride Lipase, and Free Fatty Acids in Subcutaneous Adipose Tissues throughout the Ripening Process of Dry-cured Ham. Ames (Iowa): Iowa State University, January 2011. http://dx.doi.org/10.31274/ans_air-180814-1025.

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Yang, Lin, Yanzhu Liu, Trudy M. Forte, Jeffrey W. Chisholm, John S. Parks, and Neil S. Shachter. Cultured human astrocytes secrete large cholesteryl ester- andtriglyceride-rich lipoproteins along with endothelial lipase. Office of Scientific and Technical Information (OSTI), December 2003. http://dx.doi.org/10.2172/886608.

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Quiroga, Ariel D., and Richard Lehner. Acylglycerol Lipases (Neutral Lipid Hydrolysis). AOCS, June 2011. http://dx.doi.org/10.21748/lipidlibrary.39188.

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López Tejero, M. Dolores. La Lipoproteína Lipasa: una enzima peculiar y cinco problemas metabólicos que resolver. Sociedad Española de Bioquímica y Biología Molecular (SEBBM), November 2016. http://dx.doi.org/10.18567/sebbmdiv_rpc.2016.11.1.

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Narayan, K. A., Amalia Neidhardt, Susan Sundaram, and Jason Kupperschmidt. Factors Influencing the Digestibility of Solid Fats: Mammalian and Plant Lipases--Glyceride Structure and Solvent. Fort Belvoir, VA: Defense Technical Information Center, May 1993. http://dx.doi.org/10.21236/ada265840.

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Marsh, Charles P., Thomas A. Carlson, Robert A. Weber, Carl A. Feickert, and Peter B. Stynoski. Lipari Landfill Piping Network Corrosion Condition Assessment and Service Life Prediction Analysis. Fort Belvoir, VA: Defense Technical Information Center, December 2008. http://dx.doi.org/10.21236/ada500700.

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WARWICK UNIV COVENTRY (UNITED KINGDOM). Lipases: Structure, Function and Applications in Biotransformations: A Descriptive Summary of an International Conference Held in Coventry (United Kingdom) on 16-18 July 1991. Fort Belvoir, VA: Defense Technical Information Center, July 1991. http://dx.doi.org/10.21236/ada243010.

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Jefferson, C. W., T. Peterson, V. Tschirhart, W. Davis, J. M J Scott, K. Reid, P. Raemaekers, et al. LIPS and Proterozoic uranium (U) deposits of the Canadian Shield. Natural Resources Canada/ESS/Scientific and Technical Publishing Services, 2013. http://dx.doi.org/10.4095/292377.

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Ernst, R. E., and L. J. Hulbert. Background Pt-Pd levels in mafic large igneous provinces (LIPs) in Canada. Natural Resources Canada/ESS/Scientific and Technical Publishing Services, 2003. http://dx.doi.org/10.4095/214416.

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Ruiz, Nancy, and Meng-Dawn Cheng. Aerosol Beam Focused-Laser Induced Plasma Spectrometer (ABF-LIPS) Continuous Emissions Multi-Metals Analyzer. Fort Belvoir, VA: Defense Technical Information Center, June 2012. http://dx.doi.org/10.21236/ada573127.

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