Relevant bibliographies by topics / Lipases

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  2. Dissertations / Theses
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Academic literature on the topic 'Lipases'

Author: Grafiati
Published: 4 June 2021
Last updated: 22 June 2024

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Journal articles on the topic "Lipases"

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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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Wei, Xianqin, Jiaxing Li, Tao Wang, Jinhua Xiao, and Dawei Huang. "Genome-Wide Identification and Analysis of Lipases in Fig Wasps (Chalcidoidea, Hymenoptera)." Insects 13, no. 5 (April 24, 2022): 407. http://dx.doi.org/10.3390/insects13050407.

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Lipases are the main enzymes involved in lipid metabolism. However, the characteristics of lipases in insects were scarcely investigated. Here, we screened the recently sequenced genomes of 12 fig wasp species consisting of seven pollinator fig wasps (PFWs) and five non-pollinating fig wasps (NPFWs) for the six major lipase gene families. In total, 481 lipase genes were identified, and the two most numerous families were the neutral and acid lipases. Tandem duplication accounted for the expansion of the gene family. NPFWs had significantly more lipases than PFWs. A significant gene family contraction occurred in the clade of PFWs. The difference of lipases between NPFWs and PFWs might contribute to their distinction in life histories and feeding regimes. Phylogenetic analysis showed that the lipase genes of each fig wasp species was almost equally distributed in each clade, indicating that the lipase genes were conserved. The gene structures were similar within each clade, while they were different among clades. Most of the neutral and acid lipases were signal peptides and located extracellularly. The pathways of lipases involved were predicted. This genome-wide study provides a systematic analysis of lipase gene families in 12 hymenopteran insects and further insights towards understanding the potential functions of lipases.
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Bassegoda, Arnau, F. I. Javier Pastor, and Pilar Diaz. "Rhodococcus sp. Strain CR-53 LipR, the First Member of a New Bacterial Lipase Family (Family X) Displaying an Unusual Y-Type Oxyanion Hole, Similar to the Candida antarctica Lipase Clan." Applied and Environmental Microbiology 78, no. 6 (January 6, 2012): 1724–32. http://dx.doi.org/10.1128/aem.06332-11.

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ABSTRACTBacterial lipases constitute the most important group of biocatalysts for synthetic organic chemistry. Accordingly, there is substantial interest in developing new valuable lipases. Considering the lack of information concerning the lipases of the genusRhodococcusand taking into account the interest raised by the enzymes produced by actinomycetes, a search for putative lipase-encoding genes fromRhodococcussp. strain CR-53 was performed. We isolated, cloned, purified, and characterized LipR, the first lipase described from the genusRhodococcus. LipR is a mesophilic enzyme showing preference for medium-chain-length acyl groups without showing interfacial activation. It displays good long-term stability and high tolerance for the presence of ions and chemical agents in the reaction mixture. Amino acid sequence analysis of LipR revealed that it displays four unique amino acid sequence motifs that clearly separate it from any other previously described family of bacterial lipases. Using bioinformatics tools, LipR could be related only to several uncharacterized putative lipases from different bacterial origins, all of which display the four blocks of consensus amino acid sequence motifs that contribute to define a new family of bacterial lipases, namely, family X. Therefore, LipR is the first characterized member of the new bacterial lipase family X. Further confirmation of this new family of lipases was performed after cloningBurkholderia cenocepaciaputative lipase, bearing the same conserved motifs and clustering in family X. Interestingly, all lipases grouping in the new bacterial lipase family X display a Y-type oxyanion hole, a motif conserved in theCandida antarcticalipase clan but never found among bacterial lipases. This observation contributes to confirm that LipR and its homologs belong to a new family of bacterial lipases.
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Wang, Jiale, Jiqiang Song, Qi Fang, Hongwei Yao, Fang Wang, Qisheng Song, and Gongyin Ye. "Insight into the Functional Diversification of Lipases in the Endoparasitoid Pteromalus puparum (Hymenoptera: Pteromalidae) by Genome-scale Annotation and Expression Analysis." Insects 11, no. 4 (April 5, 2020): 227. http://dx.doi.org/10.3390/insects11040227.

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Lipases play essential roles in digestion, transport, and processing of dietary lipids in insects. For parasitoid wasps with a unique life cycle, lipase functions could be multitudinous in particular. Pteromalus puparum is a pupal endoparasitoid of butterflies. The female adult deposits eggs into its host, along with multifunctional venom, and the developing larvae consume host as its main nutrition source. Parasitoid lipases are known to participate in the food digestion process, but the mechanism remains unclear. P. puparum genome and transcriptome data were interrogated. Multiple alignments and phylogenetic trees were constructed. We annotated a total of 64 predicted lipase genes belonging to five lipase families and suggested that eight venom and four salivary lipases could determine host nutrition environment post-parasitization. Many putative venom lipases were found with incomplete catalytic triads, relatively long β9 loops, and short lids. Data analysis reveals the loss of catalytic activities and weak triacylglycerol (TAG) hydrolytic activities of lipases in venom. Phylogenetic trees indicate various predicted functions of lipases in P. puparum. Our information enriches the database of parasitoid lipases and the knowledge of their functional diversification, providing novel insight into how parasitoid wasps manipulate host lipid storage by using venom lipases.
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Chen, Mei, Tongtong Jin, Binbin Nian, and Wenjun Cheng. "Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art." Molecules 29, no. 11 (May 22, 2024): 2444. http://dx.doi.org/10.3390/molecules29112444.

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Lipases, crucial catalysts in biochemical synthesis, find extensive applications across industries such as food, medicine, and cosmetics. The efficiency of lipase-catalyzed reactions is significantly influenced by the choice of solvents. Polar organic solvents often result in a decrease, or even loss, of lipase activity. Conversely, nonpolar organic solvents induce excessive rigidity in lipases, thereby affecting their activity. While the advent of new solvents like ionic liquids and deep eutectic solvents has somewhat improved the activity and stability of lipases, it fails to address the fundamental issue of lipases’ poor solvent tolerance. Hence, the rational design of lipases for enhanced solvent tolerance can significantly boost their industrial performance. This review provides a comprehensive summary of the structural characteristics and properties of lipases in various solvent systems and emphasizes various strategies of protein engineering for non-aqueous media to improve lipases’ solvent tolerance. This study provides a theoretical foundation for further enhancing the solvent tolerance and industrial properties of lipases.
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Ahmad, Sana, Aliya Riaz, Hina Abbasi, Reeja Eijaz, and Muhammad Noman Syed. "Modification of Process Parameters for Enhanced Lipase Induction from Bacillus SR1." RADS Journal of Biological Research & Applied Sciences 10, no. 1 (July 16, 2019): 14–17. http://dx.doi.org/10.37962/jbas.v10i1.137.

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The enzymes catalyze the cleavage of triacylglycerols into fatty acids and glycerols are referred to as lipases (EC 3.1.1.3). Lipases are widely distributed in flora and fauna. Microbial lipases are of great importance than lipases from plants and animals due to their catalytic activity, ease of production and optimization. Lipases have tremendous industrial applications such as in the processing of fats and oils, detergents and degreasing formulations, food processing, the synthesis of fine chemicals, paper manufacture, and production of cosmetics, and pharmaceuticals. Therefore, a potential lipase producing bacterial strain was isolated and identified as gram +ve Bacillus SR1. Among different oils tested, olive oil was found to be the favorable substrate for lipase induction. Additionally, lipase induction was observed highest in 24 hours of fermentation at 37⁰C and pH 7.5.
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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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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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Cheng, Wenjun, and Binbin Nian. "Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art." Molecules 28, no. 15 (August 3, 2023): 5848. http://dx.doi.org/10.3390/molecules28155848.

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As some of the most widely used biocatalysts, lipases have exhibited extreme advantages in many processes, such as esterification, amidation, and transesterification reactions, which causes them to be widely used in food industrial production. However, natural lipases have drawbacks in terms of organic solvent resistance, thermostability, selectivity, etc., which limits some of their applications in the field of foods. In this systematic review, the application of lipases in various food processes was summarized. Moreover, the general structure of lipases is discussed in-depth, and the engineering strategies that can be used in lipase engineering are also summarized. The protocols of some classical methods are compared and discussed, which can provide some information about how to choose methods of lipase engineering. Thermostability engineering and solvent tolerance engineering are highlighted in this review, and the basic principles for improving thermostability and solvent tolerance are summarized. In the future, comput er-aided technology should be more emphasized in the investigation of the mechanisms of reactions catalyzed by lipases and guide the engineering of lipases. The engineering of lipase tunnels to improve the diffusion of substrates is also a promising prospect for further enhanced lipase activity and selectivity.
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Joshi, Ritika, and Arindam Kuila. "Lipase and their different industrial applications: A review." Brazilian Journal of Biological Sciences 5, no. 10 (2018): 237–47. http://dx.doi.org/10.21472/bjbs.051004.

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Enzymes are also known natural catalysts. Lipases are flexible enzymes that are mostly used. These enzymes are found extensively all over the animal and plant kingdoms, likewise in molds and bacteria. Among all identified enzymes, lipases have concerned the mainly biotechnological attention. This review paper discusses the characteristic, microbial origin and application of lipases. The present review discussed about different characteristics and sources (fungal, bacteria’s) of lipase. The present article also discussed about different bioreactors used for lipase production and different biotechnological applications (food, detergent, paper and pulp, biofuels etc) of lipases. An observation to considerate lipases and their applications as bulk enzymes and high-value of production, these enzymes are having huge impact in different bioprocesses.
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Dissertations / Theses on the topic "Lipases"

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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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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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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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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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Mallett, Lucy E. "Thermostable esterases and lipases." Thesis, University of Exeter, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.432880.

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Carulla, i. Sanmartí Pere. "Isoformes de pI de la lipoproteïna lipasa: Origen, distribució i funció." Doctoral thesis, Universitat de Barcelona, 2017. http://hdl.handle.net/10803/462027.

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Un dels principals aspectes que hem descrit ha estat la presència i la distribució de les isoformes de pI de l’LPL. Inicialment hem treballat amb teixits de rata adulta: cor, TAB, TAM i múscul. Els resultats han demostrat que tots els teixits de rata dels quals s’ha pogut purificar parcialment l’LPL presenten isoformes de pI de l’LPL. També hem treballat en una de les poques situacions en què el fetge expressa LPL: en cries de rata. Lamentablement, l’LPL ha resultat ser una proteïna difícilment purificable. A les cries de rata, però, hem pogut descriure clarament la presència d’isoformes de l’LPL al cor i al TAM. A partir de tota la informació obtinguda de la descripció d’isoformes en teixits de rata, hem dissenyat un mètode per modelitzar el patró d’isoformes de cada teixit, determinat pel nombre d’isoformes, i el pI i l’abundància relativa de cada isoforma. Aquesta modelització ens ha permès comparar els patrons obtinguts en cada purificació i determinar la similitud dels patrons d’isoformes entre diferents teixits i diferents espècies. La presència de les isoformes en sí ja és un fet molt important pel coneixement de l’LPL. Però el fet d’haver descrit diferències entre els patrons d’isoformes entre els teixits de rata, va posar de manifest la rellevància de la funció diferencial de l’LPL en cada teixit. A partir d’aquesta idea hem estudiat la funció de les isoformes de pI de l’LPL. Com està àmpliament descrit, l’expressió i l’activitat de l’LPL és depenent de cada teixit i de la situació fisiològica en què es trobi l’animal. Hem descrit els patrons de l’LPL de diferents teixits de rata (cor, TAB i TAM) en situacions fisiològiques en les quals és sabut que l’activitat LPL varia notablement (fred, dejuni i realimentació) respecte a la situació control. Mitjançant el pI i la abundància relativa de les isoformes de tots els teixits de rata, hem dissenyat un sistema de classificació de les isoformes en poblacions segons clústers. Aquesta caracterització de les isoformes en clústers permet descriure les variacions que hi ha entre diferents situacions o teixits des d’un enfocament totalment diferent al tractat fins aleshores. Hem pogut detectar importants variacions en les poblacions de les isoformes de pI segons la situació fisiològica. Paral·lelament, hem estudiat l’afinitat de les isoformes de pI de l’LPL tant per l’ancoratge (heparina) com pel substrat. Entre les diferents isoformes no hem descrit diferències d’afinitat per heparina i totes presenten activitat LPL. Tot i això, no podem descartar petites diferències d’afinitat pel substrat. Del TAB visceral de macaco, n’hem descrit la presència d’isoformes de pI de l’LPL i el seu patró de distribució. Totes les isoformes de pI del TAB d’aquesta espècie també presenten afinitat pel substrat i, per tant, activitat LPL. A més, també són degudes, parcialment, a la glicosilació de la proteïna. Ens hem plantejat determinar quines són les característiques que determinen l’origen les isoformes de pI de l’LPL. A partir de la purificació del TAB de macaco, hem determinat de novo d’un 74% de la seqüència de l’LPL. En aquesta cobertura, hem pogut confirmar la presència de l’asparagina 44 i les tirosines 95 i 165. Aquests aminoàcids estan descrits en altres espècies com a objectius de modificacions posttraduccionals. A continuació, hem treballat per separar les isoformes de pI, les unes de les altres, mitjançant l’isoelectroenfocament en líquid (off-gel electrophoresis). L’objectiu d’aquest treball ha estat poder treballar amb les isoformes per separat i determinar quina combinació de modificacions posttraduccionals és la responsable de cada isoforma. Novament, probablement a causa de les característiques de l’LPL, ens ha resultat impossible obtenir la purificació de cada isoforma
We have described has been the presence and distribution of the pI isoforms of LPL. We have worked with adult rat tissues: heart, WAT, BAT and muscle. The results have shown that all tissues have LPL isoforms. In 15-days old rats, the LPL expressed in the liver LPL has turned out to be a protein that is hard to purify. However, we have been able to clearly describe the presence of isoforms of LPL in heart and BAT. We have designed a method for modelling the isoform pattern of each tissue, determined by the number of isoforms, and the pI and the relative abundance of each isoform. This modelling has allowed us to compare the patterns and to determine the similarity of isoform patterns. We have studied the function of the pI isoforms of LPL. The expression and activity of the LPL is dependent on each tissue and the physiological situation in which the animal is found. We have described the LPL patterns of different rat tissues (heart, TAB and TAM) in physiological situations in which LPL activity is known to vary markedly (cold, fasting and refeeding) compared to the control animals. By means of the pI and the relative abundance of the isoforms of all the rat tissues, we have designed a system of classification of the isoforms in populations according to clusters. This characterization of isoforms in clusters allows describing the variations that exist between different situations or tissues from a totally different approach to the one treated until now. At the same time, we have studied the affinity of the pI isoforms of LPL for the anchor (heparin) and the substrate. Among the different isoforms we have not described differences in affinity and all isoforms are active. We have described the presence of pI isoforms of LPL and its distribution pattern of the WAT of Macaca fascicularis. In addition, they are also partially due to glycosylation of the protein. We have described 74% of the sequence of the LPL. In this coverage, we have been able to confirm the presence of asparagine 44 and tyrosine 95 and 165. These amino acids are described in other species as targets for posttranslational modifications.
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7

Souza, Maria Cristiane Martins de. "ImobilizaÃÃo de lipase de Candida antarctica do tipo B em nanopartÃculas magnÃticas visando a aplicaÃÃo na sÃntese de Ãsteres." Universidade Federal do CearÃ, 2013. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=9381.

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Neste trabalho, nanopartÃculas magnÃticas de ferro (Fe3O4) (NPM) foram avalia- das como suporte para a imobilizaÃÃo de lipase de Candida antarctica do tipo B (CALB). O biocatalisador (CALB-NPM) foi analisado na catÃlise dos Ãsteres: oleato de etila (biodiesel), butirato de metila e etila. NanopartÃculas magnÃticas sÃo particularmente interessantes para imobilizaÃÃo enzimÃtica devido as suas propriedades magnÃticas favorecerem a fÃcil separaÃÃo da mistura reacional atravÃs do uso de magnetismo. A enzima CALB à uma enzima capaz de atuar em diversas reaÃÃes, como, hidrÃlises e transesterificaÃÃes. Contudo, um dos problemas do uso de enzimas como catalisadores homogÃneos à a sua recuperaÃÃo. Assim, à necessÃrio o uso de suportes que retenham a enzima, mantendo suas caracterÃsticas catalÃticas. As na- nopartÃculas foram produzidas pelo mÃtodo de co-precipitaÃÃo. Determinou-se o tamanho das nanopartÃculas (11 nm) atravÃs da tÃcnica de difraÃÃo de raios-X (DRX) com posterior refi- namento das fases obtidas pelo mÃtodo Rietveld. Espectros de infravermelho foram obtidos para anÃlise de presenÃa de hidroxilas usando pastilhas de KBr das ferritas magnÃticas. O espectro foi medido na regiÃo entre 400 e 4000 cm−1. ModificaÃÃes foram realizadas na su- perfÃcie das mesmas com γ-aminopropiltrietoxissilano (APTS) e glutaraldeÃdo. No processo de imobilizaÃÃo, a influÃncia da velocidade de agitaÃÃo (20-250 rpm), carga enzimÃtica (45-200 UpNPB.g−1), tempo de contato enzima-suporte (0,5-5 h), concentraÃÃo de glutaraldeÃdo (2,5 e 25 % (m/v)), aditivo dodecil sulfato de sÃdio (SDS 0,23 %) e reutilizaÃÃo do biocatalisador fo- ram avaliadas. A imobilizaÃÃo foi realizada na presenÃa de 100 mM de tampÃo bicarbonato de sÃdio, pH 10, a 25 ÂC. ApÃs a imobilizaÃÃo, a enzima imobilizada exibiu melhor estabilidade tÃrmica e operacional do que na forma solÃvel. As condiÃÃes Ãtimas de imobilizaÃÃo foram: velocidade de agitaÃÃo de 45 rpm, carga enzimÃtica (80 UpNPB.g−1), tempo de imobilizaÃÃo de 1 h, soluÃÃo de glutaraldeÃdo (25 % (m/v)), possibilitando um rendimento de imobilizaÃÃo de 41,8 % e atividade enzimÃtica do derivado de 29,1 UpNPB/g. AlÃm disso, o biocatalisador manteve aproximadamente, 53% de atividade catalÃtica inicial apÃs cinco ciclos consecutivos de reaÃÃo hidrolÃtica. ApÃs a imobilizaÃÃo, a estabilidade tÃrmica dos derivados foi realizada a partir da reaÃÃo de hidrÃlise com 0,01 g de CALB-NPM. atividade catalÃtica da enzima livre e imobilizada foi analisada a 60 ÂC. A produÃÃo de esteres foi realizada com o biocatalisador na melhor condiÃÃo catalÃtica. AlÃm das nanopartÃculas foram analisadas a bioconversÃo de esteres por resinas acrÃlicas comerciais (CALB imobilizada). A conversÃo de oleato de etila foi de aproximadamente 90% para os biocatalisadores testados. Os ciclos de reaÃÃo consecutivos (14) mostram a manutenÃÃo da produÃÃo de biodiesel. A mÃxima conversÃo de buitrato de etila (96,8%) e metila (93,9%) foram obtidos apÃs 8 h de reaÃÃo a 25 ÂC com CALB imobilizada em nanopartÃculas magnÃticas. Os ciclos de reaÃÃo consecutivos (12) mostram a manutenÃÃo da produÃÃo dos Ãsteres (aproximadamente 76% para as nanopartÃculas e 79% para a resina acrÃlica).
In this work, magnetic nanoparticles of iron (Fe3O4) (NPM) were evaluated as a support for the immobilization of lipase Candida antarctica B (CALB). The biocatalyst (CALB- NPM) was analyzed in the catalysis of esters: ethyl oleate (biodiesel), methyl and ethyl buty- rate. Magnetic nanoparticles are particularly interesting for enzyme immobilization due to their magnetic properties favoring the easy separation from the reaction mixture by use of magne- tism. The CALB enzyme is an enzyme capable of acting in various reactions, such as hydrolysis and transesterifications. However, one problem of using enzymes as homogeneous catalysts is their recovery. Thus, it is necessary to use brackets that retain the enzyme while maintaining its catalytic characteristics. Nanoparticles were produced by co-precipitation method. We de- termined the size of the nanoparticles (11 nm) using the technique of X-ray diffraction (XRD) with subsequent refining of the phases obtained by the Rietveld method. Infrared spectra were obtained for analysis of the presence of hydroxyls using KBr pellets of magnetic ferrites. The spectrum was measured in the region between 400 and 4000 cm −1. Modifications were car- ried out on the nanoparticlesâ surfaces with γ-aminopropyltriethoxysilane (APTS) and glutaral- dehyde. The influence of stirring speed (20-250 rpm), enzyme load (45-200 UpNPB/gsupport), immobilization time (0.5-5 h), glutaraldehyde solution (2.5 and 25%), additive (SDS 0.23%) and reuse of the biocatalyst (six hydrolytic cycles reactions) were evaluated. The immobiliza- tion was performed in the presence of 100mMsodium bicarbonate buffer, pH 10, at 25 ÂC. After immobilization, CALB exhibited improved thermal and operational stabilities. The best result (Immobilization yield: 53% and immobilized enzyme activity: 29.1 UpNPB/gsupport) was obtained at 45 rpm, using 200 UpNPB/gsupport and 1h of immobilization. Furthermore, immo- bilized Calb maintained approximately 41.8 % of initial activity after five cycles of hydrolysis. The ethyl oleate production was analyzed with the best condition and compared to commercial acrylic resins (CALB immobilized). The ethyl oleate conversion was approximately 90 % for the two biocatalyst at 48 h. The consecutive reaction cycles (14) show the maintenance in the production of biodiesel. Maximum conversion of methyl butyrate (93.9 %) and ethyl butyrate (96.8 %) were achieved after 8 h of reaction at 25 ÂC for CALB immobilized onto magnetic nanoparticles. The consecutive reaction cycles (12) show the maintenance in the production of esters (approximately 76 % for nanoparticles and 79 % for acrylic resin).
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Nini, Lylia. "Etude du comportement cinétique des lipases de différentes origines sur les esters vinyliques et les triacylglycérols en solution et en émulsion : comparaison entre lipases et estérases." Aix-Marseille 3, 2002. http://www.theses.fr/2002AIX30038.

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On admet que les lipases, au contraire des estérases, agissent aux interfaces et montrent une forte augmentation d'activité en présence d'une émulsion de substrat (activation interfaciale). La structure de nombreuses lipases montre qu'il existe une boucle peptidique (volet) masquant l'accés au site actif. On a considéré ce domaine comme une caractéristique des lipases. L'étude du comportement cinétique des lipases de R. Oryzae, M. Miehei, P. Cyclopium, P. Camembertii, H. Lanuginosa, C. Rugosa, C. Antarctica, des lipases de pancréas humain et de Cobaye, de l'estérase hépatique, de l'acétylcholinestérase et de la cutinase, à l'aide d'esters vinyliques et triglycérides, a montré que toutes ces enzymes, dont certaines ne possèdent pas de volet, sont actives sur des solutions d'esters sans montrer d'activation interfaciale. Les estérases ont une très grande affinité pour les esters en solution et se distinguent des lipases par leur incapacité à hydrolyser les émulsions trioléine, la trioctanoine et laurate de vinyle
It is admitted that lipases, in contrast to esterases, act at interfaces display a high increase in activity in the presence of emulsified substrate (interfacial activation). The structure of several lipases show the existence of a peptide loop (lid) which prevents access to the active site. The lid domain has been considered as a typical feature of lipases. The study of the kinetic behaviour of lipases from R. Oryzae, M. Miehei, P. Camembertii, H. Lanuginosa, C. Rugosa, C. Antarctica, human and guinea pig pancreas, hepatic esterase, acetylcholinesterase and cutinase, with vinyl esters and triacylglycerols has shown that all lipases, some of which do not posses a lid domain and esterases are active on solutions of esters without showing interfacial activation. Esterases have a high affinity for esters in solution and differentiate from lipases by their inability to hydrolyse emulsions of triolein, trioctanoin and vinyl laurate
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Paques, Fernanda Wiermann. "Extração e caracterização da fração lipolitica de residuos de processamento de mamão formosa." [s.n.], 2005. http://repositorio.unicamp.br/jspui/handle/REPOSIP/256634.

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Orientador: Gabriela Alves Macedo
Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos
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Mestrado
Ciência de Alimentos
Mestre em Ciência de Alimentos
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Martins, Mariana Provedel. "Biotransformação de epóxidos com fungos de origem marinha e síntese de cloroidrinas." Universidade de São Paulo, 2008. http://www.teses.usp.br/teses/disponiveis/75/75131/tde-14102008-095435/.

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Neste trabalho realizou-se uma triagem com os fungos de origem marinha Trichoderma sp Gc1, Penicillium miczynskii Gc5, Penicillium raistrickii Ce16 e Aspergilus sydowii Gc12 para catalisar a abertura do (RS)-2-(benziloximetil)oxirano (2). O melhor resultado foi obtido com o fungo Trichoderma sp Gc1, pois forneceu o (R)-(-)-2-(benziloximetil)oxirano (2) com excesso enantiomérico de 60 % e rendimento isolado de 39 %; o diol (S)-(+)-1,2-propanodiol-3-fenilmetóxi (2a) com excesso enantiomérico de 32 % e rendimento de 19 %. Posteriormente otimizou-se as condições experimentais com o epóxido 2 e o fungo Trichoderma sp Gc1, variando-se a massa de biocatalisador, o meio de cultura e o tempo de reação. Os melhores resultados sob essas condições foram aplicadas para os epóxidos 3-5 fornecendo o (S)-(+)-2-[4-metoxifenoxi)metil]oxirano (3a), (S)-(+)-2-(propeniloxi)oriano (4), (R)-(+)-1-alilóxi-2,3-propanodiol (4a) e o (-)-9-deceno-1,2-diol (5a). Nesses estudos embora ocorreu a abertura seletiva dos epóxidos com as células totais do fungo Trichoderma sp Gc1, não obteve-se altas purezas enantioméricas dos produtos. Ainda nesse trabalho realizou-se a síntese das cloroidrinas racêmicas, a (RS)- 1-cloro-2-propanol- 3-fenilmetóxi (2b), (RS)- 1-cloro-2-propanol- 3-(4-metoxifenóxi) (3b) e (RS)- 1-alilóxi-3-cloro-2-propanol (4b) em bons rendimentos e uma metodologia sintética ambientalmente apropriada, pois os compostos foram preparados em meio aquoso na presença de íons cloreto. Em seguida realizou-se uma resolução enzimática da (RS)-1-alilóxi-3-cloro-2-propanol (4b) com a lipase de Candida antarctica onde obteve-se a clorodrina 4a (e.e. 72 %) e o seu correspondente produto acetilado 4c (e.e. 82 %) em bons excessos enantioméricos. Conclui-se que os fungos de origem marinha utilizados neste trabalho são potenciais fontes de epóxido-hidrolases para promover a abertura seletiva de epóxidos.
In this work carried out itself the first study biocatalytic involving reactions of reduction of cetonas with fungi of marine origin. They were utilized 7 cetonas commercial as substratos and 8 fungi derived little seas like biocatalisadores. The fungi were isolated of the sponges little seas Geodia corticostylifera (Trichoderma sp Gc1, Penicillium miczynskii Gc5, Aspergillus sydowii Gc12) and Chelonaplysylla erect (Bionectria sp Ce5, Aspergillus sydowii Ce15, Penicillium raistrickii Ce16 and Aspergillus sydowii Ce19). The reduction 2-chloro-1-phenylethanone (1) was studied under several conditions of reaction (changes of pH, addition or absence of glucose) and the best result was with fungus P. miczynskii Gc5, therefore itself obteve an isolated performance of 60% and excess enantiomeric of 50% for the (S)- 2-chloro-1- phenylethanol (1a). The interesting one in these studies was that all of the fungi utilized in the selection with the 2-chloro-1-phenylethanone (1) presented selectivity anti- Prelog. In the literature is common obtain reduction enzymatic with selectivity Prelog. To 2-bromo-1-phenylethanone (2) was biotransformaded by the fungus A. sydowii Ce19 you correspond composed: (S)-2-bromo-1-phenylethanol (2a), (S)-2-cloro-1- phenylethanol (1a), whereas to (2c), 2-chloro-1-phenylethanone (1) and the 2- phenyloxirane (2b) were obtained by reactions not enzymatic. To 2-bromo-1-(4- bromophenyl)ethanone (3) and to 2-bromo-1-(4-nitrophenyl)ethanone (4) were entirely biodegradadas by the fungus A. sydowii Ce19. The reduction biocatalytic of the 1-(2- iodophenyl)ethanol (5) and 1-(3-iodophenyl)ethanol (6) with the fungus Trichoderma sp Gc1 supplied the 1-(2-iodophenyl)ethanol (5a) and the 1-(3-iodophenyl)ethanol (6a) with excellent excesses enantiomeric (e.e. > 99%). It stayed verified also that the fungi derived little seas for promote the reactions of reduction by biocatalysis are going to be cultivated in water of the artificial sea.
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Books on the topic "Lipases"

1

Paul, Woolley, Petersen Steffen B, and Nordisk industrifond, eds. Lipases: Their structure, biochemistry, and application. Cambridge [England]: Cambridge University Press, 1994.

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Byron, Rubin, and Dennis Edward A, eds. Lipases. San Diego: Academic Press, 1997.

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Byron, Rubin, and Dennis Edward A, eds. Lipases. San Diego: Academic Press, 1997.

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Xavier, Malcata F., North Atlantic Treaty Organization. Scientific Affairs Division., and NATO Advanced Study Institute on Engineering of/with Lipases (1995 : Póvoa de Varzim, Portugal), eds. Engineering of/with lipases. Dordrecht: Kluwer Academic, 1996.

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Sandoval, Georgina, ed. Lipases and Phospholipases. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-600-5.

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Sandoval, Georgina, ed. Lipases and Phospholipases. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8672-9.

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Malcata, F. Xavier, ed. Engineering of/with Lipases. Dordrecht: Springer Netherlands, 1996. http://dx.doi.org/10.1007/978-94-009-1671-5.

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Mackness, M. I., and M. Clerc, eds. Esterases, Lipases, and Phospholipases. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4899-0993-0.

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N, Schumaker Verne, ed. Lipoproteins, apolipoproteins, and lipases. San Diego: Academic Press, 1994.

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Smith, D. T. Studies on thermophilic bacterial lipases. Manchester: UMIST, 1994.

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Book chapters on the topic "Lipases"

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Miller, Laura T., Lionel Stange, Charles MacVean, Jorge R. Rey, J. H. Frank, R. F. Mizell, John B. Heppner, et al. "Lipases." In Encyclopedia of Entomology, 2207. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6359-6_2059.

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Kademi, Ali, Danielle Leblanc, and Alain Houde. "Lipases." In Enzyme Technology, 297–318. New York, NY: Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-35141-4_15.

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Johri, B. N., and S. Ahmad. "Lipases." In Thermophilic Moulds in Biotechnology, 219–43. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-015-9206-2_9.

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Divakar, Soundar. "Lipases." In Enzymatic Transformation, 23–38. India: Springer India, 2012. http://dx.doi.org/10.1007/978-81-322-0873-0_3.

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Sahu, Anita, and Ruth Birner-Gruenberger. "Lipases." In Encyclopedia of Metalloproteins, 1198–207. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_49.

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Rivera, Ivanna, Juan Carlos Mateos-Díaz, and Georgina Sandoval. "Plant Lipases: Partial Purification of Carica papaya Lipase." In Lipases and Phospholipases, 115–22. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-600-5_7.

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Godtfredsen, Sven Erik. "Microbial Lipases." In Microbial Enzymes and Biotechnology, 255–74. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0765-2_7.

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Moura, Marcelo Victor Holanda, Rafael Alves de Andrade, Leticia Dobler, Karina de Godoy Daiha, Gabriela Coelho Brêda, Cristiane Dinis AnoBom, and Rodrigo Volcan Almeida. "Extremophilic Lipases." In Extremophilic Enzymatic Processing of Lignocellulosic Feedstocks to Bioenergy, 249–70. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-54684-1_13.

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Sari, T. P., Vivek Kumar Gaur, Ayon Tarafdar, Ranjana Sirohi, Raveendran Sindhu, and Amit Kumar Rai. "Microbial Lipases." In Microbial Enzymes and Metabolites for Health and Well-Being, 75–90. Boca Raton: CRC Press, 2023. http://dx.doi.org/10.1201/9781003369295-6.

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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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Conference papers on the topic "Lipases"

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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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Gonçalves, Thalita Carvalho de, Dayane Silva Cavalcante, Martina Cerqueira Pinto, Eliane Pereira Cipolatti, and Evelin Andrade Manoel. "APLICAÇÕES INDUSTRIAIS DE LIPASES IMOBILIZADAS: UM ESTUDO QUANTITATIVO." In I Congresso de Engenharia de Biotecnologia. Revista Multidisciplinar de Educação e Meio Ambiente, 2021. http://dx.doi.org/10.51189/rema/1392.

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Introdução: As enzimas são catalisadores naturais de grande interesse industrial, pois, atuam sob condições operacionais mais brandas e apresentam alta atividade, seletividade e especificidade, possibilitando a geração de produtos mais puros e livres de contaminantes. A utilização de enzimas, como as lipases, têm aumentado nos últimos anos, sobretudo em áreas como alimentos, tecidos, fármacos, de cosméticos, de biocombustíveis, dentre outras, uma vez que são capazes de catalisar reações de hidrólise, esterificação e transesterificação. Além disso, com os avanços da tecnologia do DNA recombinante, é possível produzi-las em larga escala, tornando o processo ainda mais viável. A exploração do desenvolvimento de processos sustentáveis ​​e economicamente viáveis ​​tem despertado o interesse por tecnologias como a imobilização enzimática. A busca por processos de imobilização vem crescendo durante os últimos anos, principalmente devido aos avanços biotecnológicos e ao surgimento de novos materiais e técnicas de imobilização. Objetivo: Apresentar dados estatísticos da utilização de lipases imobilizadas nos últimos 10 anos, relacionando com o suporte utilizado e tipo de imobilização. Material e métodos: Os resultados estão sendo obtidos na plataforma PubMed e Scopus , através das buscas pelas palavras-chave lipase AND Immob* AND support. As publicações foram selecionadas segundo o seguinte critério: data de publicação de 2011 a 2021 e apenas publicações em inglês. Os seguintes parâmetros serão avaliados: frequência das técnicas e suportes utilizados nos últimos anos e aplicações das lipases. Os dados estão sendo cuidadosamente avaliados utilizando o programa Excel e serão organizados através do programa VosViewer para uma melhor visualização. Resultados e discussão: O trabalho está em desenvolvimento, mas resultados prévios mostram que, do total de publicações analisadas, as lipases imobilizadas se destacam nas áreas de bioquímica, genética e biologia molecular, seguida por medicina, química, engenharia química e agricultura. A técnica de imobilização por adsorção física é a mais utilizada (75% do total). Há uma tendência no surgimento de novos materiais e novas técnicas de imobilização, como intercruzamentos e nanoflowers. Conclusão: Os dados obtidos mostram que nos últimos 10 anos houve um aumento considerável pela busca do processo de imobilização. Estudos como este podem colaborar com o desenvolvimento da área e avanço da biocatálise
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Silveira, Rafaela Lopes, Adeline Cristina Pereira Rocha, and Vivian Machado Benassi. "IMPORTÂNCIA BIOTECNOLÓGICA DAS LIPASES." In I Congresso de Engenharia de Biotecnologia. Revista Multidisciplinar de Educação e Meio Ambiente, 2021. http://dx.doi.org/10.51189/rema/1330.

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Introdução: Considerando a atual preocupação com a situação ambiental do planeta, torna-se evidente a importância do uso de tecnologias e processos de produção cada vez menos agressivos ao meio ambiente. Relacionado a isso, ressalta-se a proeminência das enzimas em comparação aos catalisadores químicos, devido as diversas vantagens que proporciona. Dentre as enzimas com potencial biotecnológico, destaca-se as lipases, que são biocatalisadoras com ocorrência em diversos organismos e apresentam características que fazem com estas sejam extremamente atraentes para aplicações biotecnológicas. Objetivos: Apresentar a importância biotecnológica e aplicabilidade das lipases. Material e métodos: Utilizou-se base de dados científicas relevantes para a exploração e construção do conhecimento. A pesquisa foi refinada em trabalhos dos últimos três anos, tendo palavras-chave definidas de acordo com o tema principal do presente estudo e áreas correlatas. Resultados: As lipases podem ser obtidas a partir de diversas espécies de vegetais, animais e microrganismos e são capazes de catalisar reações de hidrólise e síntese, tais como esterificação, transesterificação, aminólise e lactonização, além de possuir elevada estabilidade em solventes orgânicos e serem altamente específicas ao substrato de ação. Essas singularidades fomentam o potencial de aplicação industrial dessas biomoléculas, as quais são utilizadas na indústria de papel e celulose, para o tratamento da madeira; alimentícia, para a produção de queijos curados, desenvolvendo sabor e aroma específico, no melhoramento das características de massas, na modificação de óleos e gorduras de pouco valor em lipídios com particularidades mais cobiçadas; no setor têxtil, para o melhoramento do tecido e remoção de lubrificantes; na indústria de detergentes, afim de potencializar a remoção de manchas de gordura nos utensílios que forem aplicados; para a produção de fármacos e cosméticos; no tratamento de efluentes de diversos setores industriais que emitem altos teores de lipídios e ésteres em seus rejeitos e para produção de biocombustíveis como o biodiesel. Conclusão: Devido aos diferentes processos industriais as quais as lipases podem ser aplicadas, torna-se evidente o potencial biotecnológico que essas enzimas detêm. Nesse sentido, é de extrema importância o estudo de novas fontes e da otimização de processos de produção já existentes para a melhor exploração do seu potencial biotecnológico.
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Cavalcante, Dayane Silva, Thalita Carvalho, Martina Costa Cerqueira Pinto, Eliane Pereira Cipolatti, and Evelin Andrade Manoel. "UTILIZAÇÃO DE LIPASES IMOBILIZADAS NA INDÚSTRIA FARMACÊUTICA." In I Congresso de Engenharia de Biotecnologia. Revista Multidisciplinar de Educação e Meio Ambiente, 2021. http://dx.doi.org/10.51189/rema/1336.

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Introdução: A demanda por processos industriais que causem menos impacto ambiental está crescendo ao passo que as indústrias produzem insumos cada vez mais complexos. A catálise química normalmente requer condições mais agressivas, algumas vezes são menos eficientes e mais danosas ao meio ambiente quando comparadas à catálise enzimática, dessa forma, processos enzimáticos surgem como alternativas. É muito comum a utilização de enzimas imobilizadas na indústria, inclusive na produção de substâncias biologicamente ativas, como derivados farmacológicos. Uma das enzimas que vem se destacando nesses processos biocatalíticos são as lipases, principalmente por sua ampla especificidade e possibilidade de atuação em solventes orgânicos e neotéricos. Tendo em vista a produtividade dos processos de biocatálise, condições relativamente mais brandas nas quais elas podem ser empregadas, menor impacto ambiental e a enantiosseletividade das lipases, fica clara a importância da síntese enzimática para a produção de derivados farmacológicos. Objetivo: Mostrar o crescimento da síntese de derivados farmacológicos via biocatálise a partir de dados quantitativos e avaliar as técnicas de imobilização mais empregadas na área farmacêutica. Material e métodos: Os dados foram obtidos por meio das plataformas Scopus e Patent Inspiration relativos ao número de publicações e patentes nos últimos 5 anos na área. As palavras-chave utilizadas foram lipase AND immob* AND pharm* OR drug. As técnicas de imobilização, os tipos suportes e os solventes mais utilizados na área estão sendo avaliados. Resultados e discussão: Os dados obtidos indicam uma tendência de crescimento e desenvolvimento na área. É possível destacar o uso de líquidos iônicos, que aparecem em aproximadamente 50% dos resultados obtidos, evidenciando ainda mais a preocupação com a redução dos impactos ambientais, visto que estes são classificados como solventes verdes. O trabalho ainda está em desenvolvimento, os resultados estão sendo cuidadosamente avaliados e serão apresentados em sua totalidade na próxima etapa. Conclusão: Há uma tendência na busca por processos mais verdes e pelo uso de lipases na área farmacêutica. Os dados reafirmam a importância dos processos biocatalíticos, tanto na área farmacêutica, como na biotecnologia industrial de forma geral, evidenciando também uma busca pela redução dos danos ao meio ambiente.
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Silva, Jaqueline M. R. da, Maria G. Nascimento, and Sandra P. Zanotto. "Chemo-enzymatic epoxidation of -caryophyllene mediated lipases and by mycelium-bound lipases." In 14th Brazilian Meeting on Organic Synthesis. São Paulo: Editora Edgard Blücher, 2013. http://dx.doi.org/10.5151/chempro-14bmos-r0187-2.

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Pinotti, Laura Marina, Marina de Oliveira, Juliano Xavier Lacerda, Rogério Teixeira, Celson Rodrigues, and Sérvio Túlio Alves Cassini. "PRODUÇÃO DE LIPASES POR CEPAS FÚNGICAS." In Simpósio Nacional de Bioprocessos e Simpósio de Hidrólise Enzimática de Biomassa. Campinas - SP, Brazil: Galoá, 2015. http://dx.doi.org/10.17648/sinaferm-2015-32449.

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LIMA, R. C., H. N. L. SILVA, and L. M. PINOTTI. "PRODUÇÃO DE LIPASES POR Penicillium sp." In X Congresso Brasileiro de Engenharia Química. São Paulo: Editora Edgard Blücher, 2014. http://dx.doi.org/10.5151/chemeng-cobec-ic-07-eb-138.

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SILVA, H. N. L., R. C. LIMA, and L. M. PINOTTI. "PRODUÇÃO DE LIPASES POR Bacillus megaterium." In X Congresso Brasileiro de Engenharia Química. São Paulo: Editora Edgard Blücher, 2014. http://dx.doi.org/10.5151/chemeng-cobec-ic-07-eb-136.

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OLIVEIRA, M. M., and L. M. PINOTTI. "PRODUÇÃO DE LIPASES POR RHIZOMUCOR SP." In XI Congresso Brasileiro de Engenharia Química em Iniciação Científica. São Paulo: Editora Edgard Blücher, 2015. http://dx.doi.org/10.5151/chemeng-cobeqic2015-047-31966-262447.

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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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Reports on the topic "Lipases"

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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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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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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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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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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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