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Journal articles on the topic 'Lipase'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

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 f

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2

Bracco, Paula, Nelleke van Midden, Epifanía Arango, et al. "Bacillus subtilis Lipase A—Lipase or Esterase?" Catalysts 10, no. 3 (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 dist

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3

Wang, Shang, Yan Xu, and Xiao-Wei Yu. "Micro-Aqueous Organic System: A Neglected Model in Computational Lipase Design?" Biomolecules 11, no. 6 (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 i

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4

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 (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

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5

Sholeha, Rofiqotus, and Rudiana Agustini. "LIPASE BIJI-BIJIAN DAN KARAKTERISTIKNYA." Unesa Journal of Chemistry 10, no. 2 (2021): 168–83. http://dx.doi.org/10.26740/ujc.v10n2.p168-183.

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Abstrak. Kebutuhan enzim sebagai biokatalis dalam bidang industri saat ini sangat tinggi. Jenis enzim yang bermacam-macam dan dari berbagai sumber telah banyak diteliti dan dikembangkan. Salah satu jenis enzim yang terus diteliti dan dikembangkan adalah lipase. Lipase adalah enzim golongan hidrolase yang mengkatalisis proses hidrolisis trigliserida menjadi gliserol dan asam lemak bebas.Lipase dapat ditemukan dalam berbagai sumber seperti pada mikroorganisme, hewan dan tumbuhan. Lipase banyak digunakan pada industri makanan, detergen, minyak, biodiesel dan farmasi. Artikel ini memaparkan bebera

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6

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 (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 ide

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7

Lestari, Puji, Santi Nur Handayani, and Oedjijono Oedjijono. "SIFAT-SIFAT BIOKIMIAWI EKSTRAK KASAR LIPASE EKSTRASELULER DARI BAKTERI Azospirillum sp. JG3." Molekul 4, no. 2 (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

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8

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 (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

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9

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 (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 sug

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10

Veloso, Elizabeth Cristina Tavares, Thamires Maciel de Lima Oliveira Da Silva, João Paulo da Silva Queiroz Menezes, et al. "Activated carbon from sugarcane bagasse as support for lipase immobilization by physical adsorption technique." Cuadernos de Educación y Desarrollo 16, no. 1 (2024): 588–612. http://dx.doi.org/10.55905/cuadv16n1-032.

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Lipases are recognized as the most important group of catalysts in biotechnology. However, utilization of free enzymes is often hampered by the need for more operational stability, high cost, and non-reusability. Most of these obstacles can be solved by lipase immobilization. This work's objective was to evaluate the performance of the activated carbon obtained from sugarcane straw (SAC) as a support for lipase immobilization. Two lipases were immobilized by physical adsorption on SAC: Aspergillus niger 11T53A14 lipase and CalB (lipase B from Candida antarctica, Novozymes). Results revealed th

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11

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 (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 concentr

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12

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 (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 cont

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13

Bodhak, Dorothy, and Priya Sundarrajan. "Characterization of lipase from lipase-producing bacteria and its application in the reduction of triglyceride content in milk sample." Research Journal of Biotechnology 17, no. 11 (2022): 118–26. http://dx.doi.org/10.25303/1711rjbt1180126.

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Lipases hydrolyse esters of long-chain fatty acids. They have several biotechnological applications such as in the field of food technology, leather, cosmetics, detergents, textiles, oleochemicals, pharmaceuticals and industrial waste. Lipases occur widely in nature in animals, plants and microorganisms; however, in terms of commercial significance, microbial lipases are the most beneficial owing to the ease of production. This study aimed to characterise lipase isolated from lipase-producing bacteria, which were screened on Tributyrin agar to confirm lipase production. Growth parameters of th

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14

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 (2004): 267–73. http://dx.doi.org/10.1016/j.chroma.2004.03.058.

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15

Stathopoulou, Panagiota M., Alexander L. Savvides, Amalia D. Karagouni, and Dimitris G. Hatzinikolaou. "Unraveling the Lipolytic Activity of Thermophilic Bacteria Isolated from a Volcanic Environment." BioMed Research International 2013 (2013): 1–13. http://dx.doi.org/10.1155/2013/703130.

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In a bioprospecting effort towards novel thermostable lipases, we assessed the lipolytic profile of 101 bacterial strains isolated from the volcanic area of Santorini, Aegean Sea, Greece. Screening of lipase activity was performed both in agar plates and liquid cultures using olive oil as carbon source. Significant differences were observed between the two screening methods with no clear correlation between them. While the percentage of lipase producing strains identified in agar plates was only 17%, lipolytic activity in liquid culture supernatants was detected for 74% of them. Nine strains e

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16

Knezevic, Zorica, Slavica Siler-Marinkovic, and Ljiljana Mojovic. "Immobilized lipases as practical catalysts." Acta Periodica Technologica, no. 35 (2004): 151–64. http://dx.doi.org/10.2298/apt0435151k.

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Attractive features of lipase systems include versatility, substrate selectivity, regioselectivity, enantioselectivity and catalysis at ambient temperatures and pressures. To fully exploit the technical and economical advantages of lipases, it is recommended to use them in an immobilized form to reduce the cost and the poor stability of the free lipase. This paper summarizes various methods of lipases immobilization including covalent attachment to or adsorption on solid supports, encapsulation and entrapment within the membrane and in polymeric matrices. The effects of immobilization conditio

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17

Mala, John Geraldine Sandana, and Satoru Takeuchi. "Understanding Structural Features of Microbial Lipases–-An Overview." Analytical Chemistry Insights 3 (January 2008): ACI.S551. http://dx.doi.org/10.4137/aci.s551.

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The structural elucidations of microbial lipases have been of prime interest since the 1980s. Knowledge of structural features plays an important role in designing and engineering lipases for specific purposes. Significant structural data have been presented for few microbial lipases, while, there is still a structure-deficit, that is, most lipase structures are yet to be resolved. A search for ‘lipase structure’ in the RCSB Protein Data Bank ( http://www.rcsb.org/pdb/ ) returns only 93 hits (as of September 2007) and, the NCBI database ( http://www.ncbi.nlm.nih.gov ) reports 89 lipase structu

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18

Faradis, Taritsu Hazal, Meilynda Pomeistia, Nurul Hasan Basri, Jannatin 'Ardhuha, Erin Ryantin Gunawan, and Lalu Rudyat Telly Savalas. "Biochemical Characterization of Ketapang Lipase: Its Preference to Short-Chain Fatty Acids despite the Long-Chain Fatty Acids Dominant Content." Molekul 18, no. 2 (2023): 321. http://dx.doi.org/10.20884/1.jm.2023.18.2.8302.

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Lipases are versatile enzymes with high specificity toward lipid substrate. They have many industrial applications, such as in food, pharmacy, and green fuel. So far, most explored lipases are from microbial and animal sources, whereas those from plants are less studied. The present study aims to characterize ketapang (Terminalia catappa Linn) lipase. The lipase was isolated from germinating ketapang seeds. The activity was determined by hydrolysis of virgin coconut oil (VCO). Biochemical characterization of ketapang lipase includes the optimum temperature, pH, kinetics, metal ions addition, a

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19

Istyami, Astri Nur, Myra Wardati Sari, Cristy Hagi Gultom, Tirto Prakoso, and Tatang Hernas Soerawidjaja. "Exploration of Novel Lipase from Plant Seeds and Plant Latexes." Indonesian Journal of Chemical Research 12, no. 1 (2024): 1–8. http://dx.doi.org/10.30598/ijcr.2024.12-ist.

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As the demand for fatty acids increases, the enzymatic process of triglyceride hydrolysis emerges as a promising technology. Compared to microbial lipase, utilization of plant lipase is more practical due to its ease of preparation and cost-efficiency. This work aimed to verify the degree of lipolysis of several novel lipase sources from plants. Novel lipase sources investigated were seeds of kapok (Ceiba pentandra), java almond (Sterculia foetida), pongam (Milletia pinnata), sea mango (Cerbera manghas), tamanu (Calophyllum inophyllum), latex of sea mango, aveloz (Euphorbia tirucalli), and jac

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Jacobsen, Tomas, and Otto M. Poulsen. "Separation and characterization of 61- and 57-kDa lipases from Geotrichum candidum ATCC 66592." Canadian Journal of Microbiology 38, no. 1 (1992): 75–80. http://dx.doi.org/10.1139/m92-012.

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Two lipolytic proteins (61 and 57 kDa) present in a Sephadex G-100 fraction of extracellular lipase from Geotrichum candidum ATCC 66592 were separated using high-performance liquid chromatography. Crossed electrofocusing immunoelectrophoresis was used to demonstrate that the 61-kDa lipase fraction contained two forms of lipase with pI 4.5 and 4.7. However, when deglycosylated with endoglycosidase H, the two forms gained an identical pI, 4.6. The 57-kDa lipase fraction contained one form of lipase with pI close to 4.5. Although the 61- and 57-kDa lipases were immunologically identical, the subs

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Akossi, Moya Joëlle Carole, Konan Edmond Kouassi, Abollé Abollé, Wennd Kouni Igor Ouedraogo, and Kouassi Benjamin Yao. "Transesterification of Crude Rubber Oil Catalyzed by Lipase Extract Powder of Germinated Rubber Kernels for Biodiesel Production." Energies 18, no. 5 (2025): 1252. https://doi.org/10.3390/en18051252.

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Lipases are essential in many industrial processes. Although microbial lipases are widely used, plant lipases remain more accessible and abundant, particularly in germinated kernels. This study aims to evaluate the catalytic potential of lipase extract powder of germinated rubber kernels in transesterification reaction. Germinated rubber kernels, lipase extract powder of germinated rubber kernels, and crude oils of palm (PKO), Jatropha curcas (JCO), and rubber (RSO) were characterized. The presence of lipase in the plant extract powder was evidenced by FT-IR and SEM-EDX analyses and hydrolysis

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22

Abdul Rahman, Mohd Basyaruddin, Mahiran Basri, Mohd Zobir Hussein, Raja Nor Zaliha Raja Abdul Rahman, Yau Kim Yan, and Abu Bakar Salleh. "Activated Carbon as Support for Lipase Immobilization." Eurasian Chemico-Technological Journal 5, no. 2 (2007): 115. http://dx.doi.org/10.18321/ectj298.

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Lipase from<em> Candida rugosa</em> was immobilized onto four different types of activated carbon; KI/2030, KI/3040, KI/5060 and KI/6070. The immobilized lipase was used in the esterification of oleic acid and 1-butanol in hexane. The effects of difference pore sizes, surface area, reaction temperature, thermostability of the immobilized lipases, storage stability in organic solvent and leaching studies were investigated. Among the four samples, KI/6070 gave the highest activities and stability in all the parameters investigated. Immobilized lipases generally exhibit activities hig

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El Okki, A. A. K.-E. H., S. Djekrif–Dakhmouche, L. Bennamoun, M. E. H. El Okki, and F. Z. K. Labani. "Statistical Optimization of Lipase Production by Aspergillus oryzae Using Olive Mill Wastewater." Acta Microbiologica Bulgarica 40, no. 3 (2024): 373–82. http://dx.doi.org/10.59393/amb24400312.

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Among different sources of lipases, fungal lipases are hydrolytic enzymes owing much importance in industrial applications. However, the high production cost limits the industrial application of lipases. To address this issue, we have attempted to optimize lipase production by Aspergillus oryzae on olive mill wastewater (OMW) based medium. Media optimization is considered one of the best ways to economically produce a large quantity of lipase. The medium components were optimized by a statistical approach for optimal lipase production. The Plackett–Burman design was applied to identify the sig

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Valek, Tomas, Adam Kostelnik, Pavla Valkova, and Miroslav Pohanka. "Indoxyl Acetate as a Substrate for Analysis of Lipase Activity." International Journal of Analytical Chemistry 2019 (December 1, 2019): 1–7. http://dx.doi.org/10.1155/2019/8538340.

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Lipases play a crucial role in metabolism of microbes, fungi, plants, and animals, and in analytical chemistry, they are often used in detection of fats and triglycerides. Determination of lipase activity is also important in toxicology, when lipase activity can be both increased and decreased by organophosphates and other pesticides and in medicine for diagnosis of heart diseases. The standard method for lipase activity determination is based on cleaving ester bonds in lipase buffer containing Tween. Our aim was to find a method with faster and more sensitive response. It is known that acetyl

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Høegh, Inge, Shamkant Patkar, Torben Halkier, and Mogens T. Hansen. "Two lipases from Candida antarctica: cloning and expression in Aspergillus oryzae." Canadian Journal of Botany 73, S1 (1995): 869–75. http://dx.doi.org/10.1139/b95-333.

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The basidiomycetous yeast Candida antarctica expresses two lipases that possess widely different properties. The genes LIPA and LIPB encoding both lipases were cloned and sequenced. Both lipases were secreted efficiently from Aspergillus oryzae transformed with lipase expression plasmids. N-Glycosylation was slightly more extensive in the heterologously expressed enzymes than in those purified from C. antarctica, but the enzymatic characteristics were retained. Both enzymes are encoded as preproenzymes. Proteolytic processing of the primary translation product was efficient in A. oryzae and re

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Stamenkovic, Olivera, Miodrag Lazic, Vlada Veljkovic, and Dejan Skala. "Biodiesel production by enzyme-catalyzed transesterification." Chemical Industry 59, no. 3-4 (2005): 49–59. http://dx.doi.org/10.2298/hemind0504049s.

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The principles and kinetics of biodiesel production from vegetable oils using lipase-catalyzed transesterification are reviewed. The most important operating factors affecting the reaction and the yield of alkyl esters, such as: the type and form of lipase, the type of alcohol, the presence of organic solvents, the content of water in the oil, temperature and the presence of glycerol are discussed. In order to estimate the prospects of lipase-catalyzed transesterification for industrial application, the factors which influence the kinetics of chemically-catalysed transesterification are also c

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Nolasco-Soria, Héctor, Carlos Alfonso Alvarez-González, Dariel Tovar-Ramírez, Jorge González-Bacerio, Alberto del Monte-Martínez, and Fernando Vega-Villasante. "Optimization of Classical Lipase Activity Assays for Fish Digestive Tract Samples." Fishes 9, no. 7 (2024): 261. http://dx.doi.org/10.3390/fishes9070261.

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Fish possess lipases from embryonic development to adulthood. Lipase activity methods vary and significantly differ in terms of the concentration of the substrate used, bile salt, Ca2+, temperature, pH, and type of lipase units, which limits comparative studies. The three most-used substrates are p-nitrophenyl (p-NP), β-naphthyl (β-N) derivates, and emulsified natural oils. These were selected to be redesigned in this study to measure lipase activity under temperature, pH, ion, and bile salt conditions closer to fish physiology, using the appropriate molar absorption coefficient to calculate t

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Cygler, Miroslaw, Pawel Grochulski, and Joseph D. Schrag. "Structural determinants defining common stereoselectivity of lipases toward secondary alcohols." Canadian Journal of Microbiology 41, no. 13 (1995): 289–96. http://dx.doi.org/10.1139/m95-199.

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In this review we summarize some aspects of the enantiopreference of the lipase from Candida rugosa following structural analysis of complexes of this lipase with two enantiomers of an analog of a tetrahedral intermediate in the hydrolysis of simple esters. The analysis of the molecular basis of the enantiomeric differentiation suggests that these results can be generalized to a large class of lipases and esterases. We also summarize our experiments on identification of the key regions in the lipases from Geotrichum candidum lipase responsible for differentiation between fatty acyl chains.Key

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Souza, Aline Habibe de, Mylla F. C. de Moura, Rafaelle C. B. Franson, et al. "Selection of Yarrowia lipolytica Lipases for Efficient Ester Synthesis or Hydrolysis." Reactions 5, no. 4 (2024): 1027–41. https://doi.org/10.3390/reactions5040054.

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The species Yarrowia lipolytica is an aerobic yeast that produces different lipase isoforms, including extracellular, intracellular, and membrane-bound ones. The immobilization of lipases, such as those from Y. lipolytica, increases enzyme stability and lowers operational costs, through its reuse. The characterization of those biocatalysts is highly important to orientate their technological applications. The present work aims to obtain different Y. lipolytica lipases, through fermentation and immobilization techniques, and to evaluate the ester synthesis and hydrolysis activity of these bioca

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Albayati, Samah Hashim, Malihe Masomian, Siti Nor Hasmah Ishak, et al. "Main Structural Targets for Engineering Lipase Substrate Specificity." Catalysts 10, no. 7 (2020): 747. http://dx.doi.org/10.3390/catal10070747.

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Microbial lipases represent one of the most important groups of biotechnological biocatalysts. However, the high-level production of lipases requires an understanding of the molecular mechanisms of gene expression, folding, and secretion processes. Stable, selective, and productive lipase is essential for modern chemical industries, as most lipases cannot work in different process conditions. However, the screening and isolation of a new lipase with desired and specific properties would be time consuming, and costly, so researchers typically modify an available lipase with a certain potential

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Fernandez-Lopez, Laura, Sergi Roda, Ana Robles-Martín, et al. "Enhancing the Hydrolytic Activity of a Lipase towards Larger Triglycerides through Lid Domain Engineering." International Journal of Molecular Sciences 24, no. 18 (2023): 13768. http://dx.doi.org/10.3390/ijms241813768.

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Lipases have valuable potential for industrial use, particularly those mostly active against water-insoluble substrates, such as triglycerides composed of long-carbon chain fatty acids. However, in most cases, engineered variants often need to be constructed to achieve optimal performance for such substrates. Protein engineering techniques have been reported as strategies for improving lipase characteristics by introducing specific mutations in the cap domain of esterases or in the lid domain of lipases or through lid domain swapping. Here, we improved the lipase activity of a lipase (WP_07574

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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 (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 prefer

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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 (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 enginee

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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 (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

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Fernandez-Lopez, Laura, Sergi Roda, A. Robles-Martín, et al. "Enhancing the Hydrolytic Activity of a Lipase towards Larger Triglycerides through Lid Domain Engineering." International Journal of Molecular Sciences 24, no. 18 (2023): 13768. https://doi.org/10.3390/ijms241813768.

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Lipases have valuable potential for industrial use, particularly those mostly active against water-insoluble substrates, such as triglycerides composed of long-carbon chain fatty acids. However, in most cases, engineered variants often need to be constructed to achieve optimal performance for such substrates. Protein engineering techniques have been reported as strategies for improving lipase characteristics by introducing specific mutations in the cap domain of esterases or in the lid domain of lipases or through lid domain swapping. Here, we improved the lipase activity of a lipase (WP_07574

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RN, Patel, A. Banerjee, Ko RY, et al. "Enzymic preparation of (3R‐cis)‐3‐(acetyloxy)‐4‐phenyl‐2‐azetidinone: a taxol side‐chain synthon." Biotechnology and Applied Biochemistry 20, no. 1 (1994): 23–33. http://dx.doi.org/10.1111/j.1470-8744.1994.tb00304.x.

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A key chiral intermediate [(3R‐cis)‐3‐(acetyloxy)‐4‐phenyl‐2‐azetidinone (2)] for the semi‐synthesis of paclitaxel (taxol; 5), an anti‐cancer compound, was prepared by an enzymic process. The stereoselective enzymic hydrolysis of cis‐3‐(acetyloxy)‐4‐phenyl‐2‐azetidinone (1) to the corresponding (S)‐(‐)‐alcohol (3) was carried out using various lipases. Lipase PS‐30 (Pseudomonas cepacia) and BMS (Bristol‐Myers Squibb) lipase (Pseudomonas sp. SC13856) catalysed hydrolysis of the undesired enantiomer of racemic compound 1, producing the (S)‐(‐)‐alcohol (3) and the desired (R)‐(+)‐acetate (2). Rea

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Berdiev, Nodir Sh, Jamolitdin F. Ziyavitdinov, Akmal M. Asrorov, Shukhratjon S. Olimjonov, and Shavkat I. Salikhov. "Characterization of a novel lipase from Pseudomonas aeruginosa." Nova Biotechnologica et Chimica 18, no. 1 (2019): 44–51. http://dx.doi.org/10.2478/nbec-2019-0006.

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Abstract Lipases cleaving oils into fatty acids and glycerol are of great interest for the use in increasing the efficiency of fuels. In this work, a novel lipase from Pseudomonas aeruginosa, P. aeruginosa A12, was isolated by ion-exchange and hydrophobic chromatography. The purity of lipase was shown by electrophoresis and its molecular weight was estimated to be ~ 31.6 kDa. The whole amino acid sequence was analyzed by an LC-MS/MS method. Temperature- and pH-dependent optimum of the enzyme compiled 30 °C and 7.5, respectively. The obtained enzyme exhibited 79 % similarity of amino acid seque

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Bravo-Ruiz, Gustavo, Carmen Ruiz-Roldán, and M. Isabel G. Roncero. "Lipolytic System of the Tomato Pathogen Fusarium oxysporum f. sp. lycopersici." Molecular Plant-Microbe Interactions® 26, no. 9 (2013): 1054–67. http://dx.doi.org/10.1094/mpmi-03-13-0082-r.

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The lipolytic profile of Fusarium oxysporum f. sp lycopersici was studied by in silico search and biochemical enzyme activity analyses. Twenty-five structural secreted lipases were predicted based on the conserved pentapeptide Gly-X-Ser-X-Gly-, characteristic of fungal lipases, and secretion signal sequences. Moreover, a predicted lipase regulatory gene was identified in addition to the previously characterized ctf1. The transcription profile of thirteen lipase genes during tomato plant colonization revealed that lip1, lip3, and lip22 were highly induced between 21 and 96 h after inoculation.

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Nguyen, Van Thi Ai, Hoa Ngoc Phan, Lam Bich Tran, and Ai Tran Diem Chau. "Enzymatic hydrolysis of coconut oil using free and immobilized porcine pancreas lipases." Science and Technology Development Journal 19, no. 2 (2016): 70–77. http://dx.doi.org/10.32508/stdj.v19i2.654.

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The aim of this study is to evaluate the effect of some factors on the hydrolysis of coconut oil (CO) in the present of two kind of enzymes, the free lipases and immobilized lipases porcine pancreas. The activities of these two lipases under the optimal hydrolysis conditions was determined. The effects of factors on hydrolysis degree of coconut oil was investigated: the ratio of enzyme to substrate, the pH condition, and the temperature. The best conditions for the high hydrolysis degree in case of using lipase from porcine pancreas ascatalyst included: the ratio of the enzyme to substrate of

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Sargison, Fiona, Mariya I. Goncheva, Joana Alves, Amy Pickering, and J. Ross Fitzgerald. "Staphylococcus aureus secreted lipases do not inhibit innate immune killing mechanisms." Wellcome Open Research 5 (June 25, 2021): 286. http://dx.doi.org/10.12688/wellcomeopenres.16194.2.

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Background: Staphylococcus aureus causes an array of diseases in both humans and livestock. Pathogenesis is mediated by a plethora of proteins secreted by S. aureus, many of which remain incompletely characterised. For example, S. aureus abundantly secretes two isoforms of the enzyme lipase into the extracellular milieu, where they scavenge upon polymeric triglycerides. It has previously been suggested that lipases may interfere with the function of innate immune cells, such as macrophages and neutrophils, but the impact of lipases on phagocytic killing mechanisms remains unknown. Methods: We

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Sargison, Fiona, Joana Alves, Amy Pickering, and J. Ross Fitzgerald. "Staphylococcus aureus secreted lipases do not inhibit innate immune killing mechanisms." Wellcome Open Research 5 (December 9, 2020): 286. http://dx.doi.org/10.12688/wellcomeopenres.16194.1.

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Background: Staphylococcus aureus causes an array of diseases in both humans and livestock. Pathogenesis is mediated by a plethora of proteins secreted by S. aureus, many of which remain incompletely characterised. For example, S. aureus abundantly secretes two isoforms of the enzyme lipase into the extracellular milieu, where they scavenge upon polymeric triglycerides. It has previously been suggested that lipases may interfere with the function of innate immune cells, such as macrophages and neutrophils, but the impact of lipases on phagocytic killing mechanisms remains unknown. Methods: We

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Kumar, R. Ranjith, S. Kiran, S. Girisham, and SM Reddy. "Lipase production by three thermophilic fungi." Indian Journal of Applied Microbiology 25, no. 02 (2023): 37–46. http://dx.doi.org/10.46798/ijam.2023.v25i02.3.

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   Production of lipases by three thermophilic fungi, Thermomyces lanuginosus, Talaromyces luteus and Rhizomucor pusillus was investigated, influence of substratum, pH, temperature, carbon and nitrogen sources on lipase production was also studied. All the three fungi under study produced good amount of lipase constitutively. Lipase production was maximum at 45oC and it was thermostable.  

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Mrugesh, Khunt, and Pandhi Neepa. "Purification and Characterization of Lipase from Moderate halophiles isolated from Excreta of Wild Ass (Equus hemionus khur)." International Journal of BioSciences and Technology (IJBST) ISSN: 0974-3987 5, no. 1 (2012): 1–5. https://doi.org/10.5281/zenodo.1440937.

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<strong>ABSTRACT:</strong> Twenty-four moderate halophiles were isolated from excreta of wild ass on medium containing 10% NaCl (w/v), designated as Mk-1 to Mk-24. Three best lipase producers were judged on the basis of zone ratio on solid media were selected for further study. Extracellular lipase purification was achieved by ammonium sulfate fractionation after growing organisms in liquid media containing tributyrin as carbon source.  Maximum purification of lipase from Mk-4, Mk-18 and Mk-23 was obtained in 60%-80% saturation fraction. Extracellular lipases were active maximally in acid

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Gutiérrez-Domínguez, Denise Esther, Bartolomé Chí-Manzanero, María Mercedes Rodríguez-Argüello, et al. "Identification of a Novel Lipase with AHSMG Pentapeptide in Hypocreales and Glomerellales Filamentous Fungi." International Journal of Molecular Sciences 23, no. 16 (2022): 9367. http://dx.doi.org/10.3390/ijms23169367.

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Lipases are enzymes that hydrolyze triglycerides to fatty acids and glycerol. A typical element in lipases is a conserved motif of five amino acids (the pentapeptide), most commonly G-X-S-X-G. Lipases with the pentapeptide A-X-S-X-G are present in species of Bacillus, Paucimonas lemoignei, and the yeast Trichosporon asahii; they are usually thermotolerant and solvent resistant. Recently, while searching for true lipases in the Trichoderma harzianum genome, one lipase containing the pentapeptide AHSMG was identified. In this study, we cloned from T. harzianum strain B13-1 the lipase ID135964, r

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Nallapan Maniyam, Maegala, Anupriya Sundarajoo, Hazeeq Hazwan Azman, Nor Suhaila Yaacob, and Hasdianty Abdullah. "Effect of inoculum size, inducer and metal ion on lipase production by Rhodococcus strain UCC 0009." E3S Web of Conferences 211 (2020): 02012. http://dx.doi.org/10.1051/e3sconf/202021102012.

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Lipases are critical enzymes for industrial applications such as in the food and pharmaceutical fields. Therefore, the discovery of new lipases with enhanced characteristics are always encouraged. Thus, the present study explored the ability of a novel bacterial strain isolated from a tropical climate for lipase production. The optimization method using the one-variable-at-a-time approach was adopted to obtain increased production of lipase. The strain identified as Rhodococcus strain UCC 0009 was able to generate specific lipase activity of 11.67a ± 0.00 mU/mg at optimized conditions of 8 % (

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Smith, G. M., K. Rothwell, S. L. Wood, S. J. Yeaman, and M. Bownes. "Specificity and localization of lipolytic activity in adult Drosophila melanogaster." Biochemical Journal 304, no. 3 (1994): 775–79. http://dx.doi.org/10.1042/bj3040775.

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The triacylglycerol lipases present in adult Drosophila melanogaster have been investigated. Different lipase activities are present in various tissues in the fly. In particular, an abundant lipase activity is present in the male accessory gland. An esterase null mutant was used to confirm that the enzyme activity was due to a distinct lipase and not non-specific activity from esterase 6 which is also abundant in accessory glands. The properties of the accessory-gland lipase were investigated, and pH optima and substrate utilization suggest that it has some similarities to vertebrate bile-salt

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Ehlert, Janna, Jenny Kronemann, Nadine Zumbrägel, and Matthias Preller. "Lipase-Catalyzed Chemoselective Ester Hydrolysis of Biomimetically Coupled Aryls for the Synthesis of Unsymmetric Biphenyl Esters." Molecules 24, no. 23 (2019): 4272. http://dx.doi.org/10.3390/molecules24234272.

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Lipases are among the most frequently used biocatalysts in organic synthesis, allowing numerous environmentally friendly and inexpensive chemical transformations. Here, we present a biomimetic strategy based on iron(III)-catalyzed oxidative coupling and selective ester monohydrolysis using lipases for the synthesis of unsymmetric biphenyl-based esters under mild conditions. The diverse class of biphenyl esters is of pharmaceutical and technical relevance. We explored the potency of a series of nine different lipases of bacterial, fungal, and mammalian origin on their catalytic activities to cl

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Ramos, Margarita Díaz, Letícia Passos Miranda, Roberto Fernandez-Lafuente, William Kopp, and Paulo Waldir Tardioli. "Improving the Yields and Reaction Rate in the Ethanolysis of Soybean Oil by Using Mixtures of Lipase CLEAs." Molecules 24, no. 23 (2019): 4392. http://dx.doi.org/10.3390/molecules24234392.

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Due to the heterogeneity of oils, the use of mixtures of lipases with different activity for a large number of glycerol-linked carboxylic acids that compose the substrate has been proposed as a better alternative than the use of one specific lipase preparation in the enzymatic synthesis of biodiesel. In this work, mixtures of lipases from different sources were evaluated in their soluble form in the ethanolysis of soybean oil. A mixture of lipases (50% of each lipase, in activity basis) from porcine pancreas (PPL) and Thermomyces lanuginosus lipase (TLL) gave the highest fatty acid ethyl ester

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Liu, Can, and Jian Shi. "Understanding Lipase-Deep Eutectic Solvent Interactions Towards Biocatalytic Esterification." Catalysts 15, no. 4 (2025): 358. https://doi.org/10.3390/catal15040358.

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Deep eutectic solvents (DESs) have shown promise as a medium for extracting polar volatile fatty acids (VFAs) and in situ esterification of the extracted molecules using lipases. This solvent enhanced biocatalysis process can potentially streamline VFA separation from fermentation broth by integrating conversion and extraction steps. Two commercial lipases from Aspergillus oryzae (AoL) and Candida rugosa (CrL) were evaluated in reaction systems containing hydrophilic or hydrophobic DESs using a newly optimized lipase assay. The optimal pH for both lipases was around 5.0, with a slight reductio

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Milovanović, Jelena, Katarina Banjanac, Jasmina Nikolić, Jasmina Nikodinović-Runić, and Nevena Ž. Prlainović. "The Organic-Functionalized Silica Nanoparticles as Lipase Carriers for Biocatalytic Application: Future Perspective in Biodegradation." Catalysts 15, no. 1 (2025): 54. https://doi.org/10.3390/catal15010054.

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Over the past three decades, organic reactions catalyzed by lipase have been extensively studied. To overcome the drawbacks of free enzymes and develop new and sustainable biocatalysts, various insoluble forms of lipases were examined. Especially interesting are lipases immobilized on silica nanoparticles (SiNPs) due to their promising unique and advantageous physicochemical properties. Therefore, the present paper presents an overview of different organic functionalization methods of SiNP surfaces to create a more favorable microenvironment for lipase molecules. Given the high commercial valu

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