Relevant bibliographies by topics / Pancreatic lipase inhibitor

Academic literature on the topic 'Pancreatic lipase inhibitor'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Pancreatic lipase inhibitor"

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Winanda, Witri, Irmanida Batubara, and Yulin Lestari. "Pancreatic Lipase Inhibitory Activity of Endophytic Actinobacteria from Rhododendron spp." Biosaintifika: Journal of Biology & Biology Education 13, no. 2 (August 30, 2021): 178–84. http://dx.doi.org/10.15294/biosaintifika.v13i2.29981.

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Antiobesity medication is available as therapeutic compounds that can reduce fat digestion by the inhibition of pancreatic lipase. Actinobacteria have the potency as source of bioactive compounds with various biological function including as pancreatic lipase inhibitor. However, the potency of endophytic actinobacteria from Rhododendron spp. as source of pancreatic lipase inhibitor producer has not been reported yet. The aim of this study was to examine the potential of pancreatic lipase inhibitory activity of 23 endophytic actinobacteria from Rhododendron spp.; to characterize their colony based on morphology and molecular analysis. Screening test of pancreatic lipase inhibitor was conducted using the supernatant of endophytic actinobacteria, lipase pancreatic porcine (L3126) and p-nitrophenyl butyrate. The supernatant of selected isolates was extracted using ethyl acetate. The result showed that various inhibitory activities ranging between 0.00 until 91.69%. There were 11 out of 23 isolates that have potential as pancreatic inhibitor. Amongst them, the extract of four selected isolates, i.e. RZP 1.3, RSSB 3.2, RSS 2.1, and RJB F3.2 demonstrated inhibitory percentage of more than 80%. The RJB F3.2 extract showed to have IC50 value by 431.48 µg mL-1 compared to control, i.e. Xenical (89.07 µg mL-1). Phytochemical analysis exhibited that the extract of the selected isolates contained alkaloid which may function as pancreatic lipase inhibitor. Based on the morphological character, the selected isolates have various morphological colonies and 16S rRNA gene sequence revealed the sequence homology to Streptomyces spp. The data clearly indicate that endophytic actinobacteria from Rhododendron spp. have potency as pancreatic lipase inhibitor producer and further studies could be explored for the development of antiobesity agent.
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Mhatre, Sveeta V., Amita A. Bhagit, and Raman P. Yadav. "Proteinaceous Pancreatic Lipase Inhibitor from the Seed of Litchi chinensis." Food technology and biotechnology 57, no. 1 (2019): 113–18. http://dx.doi.org/10.17113/ftb.57.01.19.5909.

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A study of the pancreatic lipase inhibitory activity of a protein from the seed of Litchi chinensis was carried out. Protein was isolated by 70 % ammonium sulphate precipitation followed by dialysis. Lipase inhibitory activity of the protein was evaluated using both synthetic (p-nitrophenyl palmitate) and natural (olive oil) substrates. Protein at the final concentration of 100 µg/mL was able to inhibit 68.2 % pancreatic lipase on synthetic substrate and 60.0 % on natural substrate. Proteinaceous nature of the inhibitor was determined using trypsinization assay. Pancreatic lipase inhibitory protein was sensitive to 0.05 % trypsin treatment with the loss of 61.9 % activity. IC50 of this proteinaceous pancreatic lipase inhibitor was 73.1 µg/mL using synthetic substrate. This inhibitory protein was sensitive to pH, with the highest inhibitory activity at pH=8.0 and the lowest at pH=3.0. Protein was further analyzed using 10 % non-reducing sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and, interestingly, it showed the presence of a single band of (61±2) kDa when stained with Coomassie brilliant blue. The isolated protein was finally crystallized to see its homogeneity by batch crystallization method. Crystals were well formed with distinct edges. The isolated protein showed good pancreatic lipase inhibitory activity.
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Hou, W., Y. Arita, and J. Morisset. "Caerulein-stimulated arachidonic acid release in rat pancreatic acini: a diacylglycerol lipase affair." American Journal of Physiology-Cell Physiology 271, no. 5 (November 1, 1996): C1735—C1742. http://dx.doi.org/10.1152/ajpcell.1996.271.5.c1735.

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This study was performed to evaluate the effect of caerulein, a cholecystokinin analogue, on arachidonic acid (AA) release in rat pancreatic acini and to determine the cellular mechanism involved. Caerulein did not stimulate phospholipase A2 (PLA2); however, diacylglycerol (DAG) lipase activity was increased. Validity of PLA2 or DAG lipase inhibitors was confirmed by their ability to selectively inhibit PLA2 or DAG lipase activities. Caerulein increased AA release from acini prelabeled with [3H]AA both dose and time dependently. Inhibitors were used to evaluate the involvement of different signaling pathways. Mepacrine and aristolochic acid, two PLA2 inhibitors, did not inhibit caerulein-induced AA release, whereas the DAG lipase inhibitor RHC-80267 did. The phospholipase C (PLC) inhibitor U-73122 totally inhibited caerulein-induced AA release, whereas the phospholipase D (PLD) inhibitor wortmannin had no effect. Our data indicate that caerulein-induced AA release results from the combined action of PLC and DAG lipase without PLA2 or PLD activation.
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ALAGÖZ, Mehmet Abdullah, İnci Selin DOĞAN, Sıla SENER, and Zeynep ÖZDEMİR. "Synthesis, Molecular Docking and Molecular Dynamics Simulation Studies of Some Pyridazinone Derivatives as Lipase Inhibitors." Cumhuriyet Science Journal 43, no. 3 (September 30, 2022): 391–97. http://dx.doi.org/10.17776/csj.1135400.

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Human health and illness are dependent on lipases, which play a key role in maintaining cell integrity, storing fat for energy and serving as signaling molecules. In this study, 4 compounds that carry 6-phenylpyridazin-3(2H)-one main nucleus, which can be effective as lipase inhibitors, were synthesized and their structures were elucidated. The biological activity of synthesized compounds was evaluated via the porcine pancreatic lipase type II (PLL) inhibitor assay. Orlistat, a lipase inhibitor, was used as a positive control. Compound 8d was found to be the most effective compound, with an IC50 value of 32.66±2.8265 (μg/mL). In addition, molecular docking and molecular dynamics simulations studies were carried out to examine the interactions of the compounds with the target in detail. The results obtained as a result of these in silico studies were found to be compatible with the lipase inhibition effects of the compounds. It was observed that the compounds may have potential lipase inhibitory effects as a result of the substitutions of the 3-(6-oxo-3-phenylpyridazin-1(6H)-yl)propanehydrazide structure.
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Hadváry, P., H. Lengsfeld, and H. Wolfer. "Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin." Biochemical Journal 256, no. 2 (December 1, 1988): 357–61. http://dx.doi.org/10.1042/bj2560357.

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Tetrahydrolipstatin inhibits pancreatic lipase from several species, including man, with comparable potency. The lipase is progressively inactivated through the formation of a long-lived covalent intermediate, probably with a 1:1 stoichiometry. The lipase substrate triolein and also a boronic acid derivative, which is presumed to be a transition-state-form inhibitor, retard the rate of inactivation. Therefore, in all probability, tetrahydrolipstatin reacts with pancreatic lipase at, or near, the substrate binding or active site. Tetrahydrolipstatin is a selective inhibitor of lipase; other hydrolases tested were at least a thousand times less potently inhibited.
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Li, Xuan, Sayo Morita, Hiroaki Yamada, Keita Koga, Wakana Ota, Toma Furuta, Atsushi Yamatsu, and Mujo Kim. "Free Linoleic Acid and Oleic Acid Reduce Fat Digestion and Absorption In Vivo as Potent Pancreatic Lipase Inhibitors Derived from Sesame Meal." Molecules 27, no. 15 (August 1, 2022): 4910. http://dx.doi.org/10.3390/molecules27154910.

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Pancreatic lipase catalyzes the cleavage of triacylglycerols at the oil–water interface, and is known as the dominant determiner of dietary fat digestion. Reducing dietary fat digestion and absorption by modulating the activity of pancreatic lipase has become a favorable strategy to tackle obesity. Orlistat is, at present, the only pancreatic lipase inhibitor approved for the treatment of obesity; however, an array of gastrointestinal adverse effects associated with orlistat limits its tolerability. As a safe alternative to orlistat, a number of natural product-derived compounds with varying degrees of pancreatic lipase inhibitory activity have been reported. We herein reported that bioactivity-guided fractionation of sesame meal led to the identification of free linoleic acid and oleic acid as potent inhibitors of porcine pancreatic lipase in vitro with an IC50 of 23.1 µg/mL (82.4 µM) and 11.7 µg/mL (41.4 µM), respectively. In rats, a single oral dose of the mixture of these fatty acids significantly suppressed the elevation of blood triacylglycerol level following fat intake. These results substantiate the role of free linoleic acid and oleic acid as a novel class of natural product-derived functional molecules that act as pancreatic lipase inhibitors, and their potential for healthy, routine-based weight management.
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Mhatre, S., A. Bhagit, and R. P. Yadav. "IN VITRO STUDIES OF SOME EDIBLE SPICES ON PANCREATIC LIPASE INHIBITORY ACTIVITY." INDIAN DRUGS 54, no. 02 (February 25, 2017): 62–68. http://dx.doi.org/10.53879/id.54.02.10815.

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Pancreatic lipase inhibitory effect of some edible spices in light of percent inhibition, efficacy, reversibility/ irreversibility and effect of pH on inhibition is presented here. Lipase inhibitory activities of methanolic extracts of eighteen spices were evaluated. Extracts of Zanthoxylum armatum, Cinnamomum tamala, Syzygium aromaticum and Myristica fragrans were considered to be of high potency in synthetic substrate assay. Only Syzygium aromaticum showed high potency in natural substrate based lipase assay. Zanthoxylum armatum extract displayed lowest IC50 of 9.0 μg/mL. On dialysis, all extracts lost their lipase inhibitory activity indicating reversible nature of inhibition. pH significantly affected the performance of spice extracts during inhibition of pancreatic lipase. Most of the extracts lost their pancreatic lipase inhibitory activity at pH 3.0 with the exception of Brassica nigra and Cinnamomum tamala. Results showed spice are good source of pancreatic lipase inhibitor and its potential as drug for obesity can be explored by addressing various issues.
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Rathod, Priyanka, Chandana Kulkarni, and Raman P. Yadav. "ANTI-DIABESITY PRINCIPLE FROM THE SEEDS OF PHYLLANTHUS EMBLICA L." INDIAN DRUGS 57, no. 12 (April 20, 2021): 41–50. http://dx.doi.org/10.53879/id.57.12.12323.

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In recent years, pancreatic lipase inhibitor and α- glucosidase inhibitor have been highlighted as potential anti-diabesity principles. In the present study, seeds of Phyllanthus emblica L. (Family: Phyllanthaceae) was studied for anti-diabesity potential in terms of pancreatic lipase inhibitory activity, α-glucosidase inhibitory activity and antioxidant activity. At 100μg/ml concentration, pancreatic lipase inhibition of the methanolic extract using synthetic substrate obtained was 73.2±0.1% (IC50 59.1μg/ml), whereas pancreatic lipase inhibition using natural substrate was 87.9 ± 2.62%. α- glucosidase inhibition of the extract at 50μg/ml was measured as 94.4±0.37% (IC50 34.4μg/ml). The superoxide scavenging activity of the extract was found to be 81.5±0.41%. Interestingly, upon TLC fingerprinting, only one band with Rf 0.70 showed multifunctional activity. The phytochemical found to be present was an alkaloid. The results evidenced the presence of multifunctional smart molecule in methanolic extract of P. emblica L and showed an alkaloid as the component responsible for anti-diabesity potential.
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Sari, Desi Ratna, Aurelia Afra, Erni Yupita Sari Br Sembiring, and Cico Jhon Karunia Simamora. "Fat-Rich Food Review on Obesity Control through Induction Enzyme Inhibitors." BIOEDUSCIENCE 5, no. 3 (December 31, 2021): 211–17. http://dx.doi.org/10.22236/j.bes/536903.

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Background: Obesity is an imbalance between height and weight due to excessive body fat tissue. The purpose of writing this review is to find out the effect of enzyme inhibitor induction on fat-rich foods as control of obesity. Method: Writing and assessing source problems related to using literature study methods. Results: One way of controlling obesity is by regulating dietary patterns and consumption of lipase inhibitors. Inhibition of lipase is one of the most widely developed effective ways in diet medicine. Inhibitory compounds cause pancreatic lipase to lose its ability in decomposition that enters the blood. The potency of plant-origin lipase inhibitor compounds can be increased in both number and performance. Increasing the production of secondary metabolite group inhibitors is by fermentation of microorganisms. Conclusion: Inhibition of triglyceride hydrolysis through inhibition of lipase enzymes can decrease and prevent obesity. Secondary metabolite induction can be fermented with microorganisms. The production of secondary metabolite compounds in medicinal plants can be increased in the presence of fermentation. Flavonoids can decrease the accumulation of lipids in the heart, reduce glucose absorption, inhibit the breakdown of polysaccharides into monosaccharides.
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Kato, Eisuke, Ai Tsuruma, Ayaka Amishima, and Hiroshi Satoh. "Proteinous pancreatic lipase inhibitor is responsible for the antiobesity effect of young barley (Hordeum vulgare L.) leaf extract." Bioscience, Biotechnology, and Biochemistry 85, no. 8 (May 28, 2021): 1885–89. http://dx.doi.org/10.1093/bbb/zbab096.

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ABSTRACT Young barley leaves (Hordeum vulgare L.) have various health effects and are employed as an ingredient in the production of health-promoting foods. Promoting antiobesity is one such health effect; however, the mechanism and bioactive compounds are unclear. In this research, young barley leaf extract (YB) was demonstrated to possess pancreatic lipase inhibitory activity. The addition of YB to a high-fat diet in mice increased fecal lipid content, indicating reduced absorption of lipids as the mechanism underlying antiobesity effect. The investigation of bioactive compounds in YB resulted in the identification of fructose–bisphosphate aldolase as a proteinous lipase inhibitor. Maximum inhibition of the protein was 45%, but inhibition was displayed at a concentration as low as 16 ng/mL, which is a characteristic inhibition compared with other reported proteinous lipase inhibitors.
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Dissertations / Theses on the topic "Pancreatic lipase inhibitor"

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Benarouche, Anais. "Etude des interactions lipase-lipides au niveau d'interfaces modèles." Thesis, Aix-Marseille, 2013. http://www.theses.fr/2013AIXM4791.

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Les enzymes lipolytiques sont solubles en phase aqueuse mais hydrolysent des substrats insolubles. Leurs activités lipolytiques dépendent donc fortement de l’organisation des substrats lipidiques présents sous forme de structures interfaciales telles que des émulsions, des micelles, des liposomes, ou des bicouches lipidiques. Les propriétés cinétiques et la spécificité de substrat de ces enzymes résultent de l’étape initiale d’adsorption à l’interface lipide-eau et des interactions entre le substrat et le site actif. Dans le cadre de ce travail de thèse, la technique des films monomoléculaires a été utilisée pour étudier en détail les étapes séquentielles d’adsorption, de catalyse et d’inhibition de l’enzyme à l’interface lipide-eau. Dans une première partie, nous avons réalisé la caractérisation physico-chimique de la lipase gastrique de chien (DGL), avec l’étude :  de son adsorption sur un film non substrat de dilauroylphosphatidylcholine ; ‚ de l’hydrolyse interfaciale de la 1,2-dicaprine dans des films mixtes en présence d’Orlistat. Concernant l’étape de catalyse, nous avons étudié l’effet du propeptide sur la spécificité de substrat et l’activité interfaciale de la phospholipase A2 sécrétée de groupe X de souris. Enfin, dans une troisième partie, nous avons comparé les propriétés interfaciales de la lipase YLLIP2 de la levure Yarrowia lipolytica qui serait un bon candidat pour l’enzymothérapie de substitution chez les patients atteints d’insuffisance pancréatique exocrine (IPE), la lipase pancréatique humaine et la DGL. Nos résultats ont confirmé le rôle d’YLLIP2 en tant qu’excellent « substitut » non seulement de la HPL en cas d’IPE, mais aussi de la DGL
Lipolytic enzymes are water-soluble whereas their substrates are insoluble in water. Their lipolytic activities depend strongly on the organization of the lipid substrates present in interfacial structures such as oil-in-water emulsions, micelles, liposomes, and membrane bilayers. The kinetic properties and substrate specificity of these enzymes result from both their adsorption at the lipid-water interface, and the interactions occurring between the substrate and the active site. In this thesis work, the monomolecular film technique was used to study in details the sequential steps of adsorption, catalysis and inhibition of model enzymes at the lipid-water interface. In a first part, we performed the physico-chemical characterization of the dog gastric lipase (DGL), by studying:  its adsorption onto a dilauroylphosphatidylcholine non-substrate film; ‚ its interfacial hydrolysis of 1,2-dicaprin in mixed films with various amounts of Orlistat. Regarding the catalysis step, we studied the effect of the propeptide on the substrate specificity and interfacial activity of the murine group X secreted phospholipase A2. A model of this enzyme with its propeptide was built from the available 3D structure of the corresponding mature human enzyme. Finally, in the third part, we compared the interfacial kinetic properties of YLLIP2 lipase of the yeast Yarrowia lipolytica which has been identified as a good candidate for enzyme replacement therapy for patients with exocrine pancreatic insufficiency (EPI), human pancreatic lipase and DGL. Our results confirmed the role of YLLIP2 as an excellent "substitute" not only for HPL in case of PEI, but also for the DGL at acidic pH values
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Chen, Tzu-Yin, and 陳姿穎. "Pancreatic lipase inhibitory activity of strictinin from raw pu-erh tea." Thesis, 2017. http://ndltd.ncl.edu.tw/handle/25189811174189895495.

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碩士
國立中興大學
生物科技學研究所
105
Tea is a common drink in daily life, drinking tea is generally considered with many health benefits, such as weight loss and reduce deposits of fat. Inhibition of lipase activity is one of the major treatment of diet-induced obesity recently. By inhibiting fat become fatty acid and monoacylglycerol, it prevent over intake of calorie. Orlistat is a clinical drug for weight loss through the mechanism which inhibit lipase activity. According to previous studies, the pu-erh tea crude extract can inhibit lipase activity. Our lab has discovered that raw pu-erh tea contained large amount of strictinin. Strictinin might be a possible cardiant as lipase inhibitor. In the beginning of this study, lipase activity inhibition was test by various kinds of tea in vitro. Preliminary evidence suggests that crude extract of raw pu-erh tea has stronger inhibitory effect than other kinds of tea. Then, strictinin was further isolated from raw pu-erh tea by Sephadex LH-20 column. In the lipase inhibition assay, Strictinin show strong lipase inhibition effect. Thus, strictinin was further tested through animal model. In olive oil tolerance test, the result indicated that the group with strictinin (130 mg/kg) administration of C57BL6 mice has lower triacylglycerol concertation in blood than the group without strictinin. In a long term experiment, the group having high-fat diet with strictinin (130 mg/kg) also has lower weight gain and less adipocyte buildup. These results indicate that strictinin in raw pu-erh tea inhibit the activity of lipase to reduce the fat uptake in food, also control the body weight. Therefore, it will have therapeutically potential to relieve metabolic syndrome.
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Auger, Mia. "Évaluation de l'effet inhibiteur de 33 espèces végétales sur la lipase pancréatique in vitro." Thesis, 2019. http://hdl.handle.net/1866/24415.

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Le diabète de type 2 et l’obésité affectent la population mondiale et, de façon disproportionnelle, chez la population adulte crie d’Eeyou Istchee. Afin de contribuer à la documentation des activités antidiabétiques de 17 plantes médicinales de la forêt boréale traditionnellement recommandées pour traiter les symptômes du diabète, cette étude procède à l’évaluation de l’activité enzymatique de la lipase pancréatique par différentes espèces de plantes. De plus, une évaluation de l’activité enzymatique de la lipase pancréatique est réalisée avec des espèces antidiabétiques de la pharmacopée urbaine de Niamey (Niger) ainsi qu’avec des baies québécoises. Enfin, des composés phénoliques sont identifiés chez ces deux derniers groupes d’espèces végétales. Les résultats de ces études démontrent que la majorité des espèces évaluées ont un effet inhibiteur sur la lipase pancréatique in vitro. Les espèces ayant démontré les plus fortes activités inhibitrices sur la lipase pancréatique sont Kalmia angustifolia, Gaultheria hispidula et Acacia nilotica. Ainsi, cette étude permet d’appuyer la justesse des connaissances traditionnelles en ajoutant la documentation d’une activité antidiabétique des espèces végétales au répertoire scientifique.
Type 2 diabetes and obesity affect the global population and, disproportionately, the adult population of the Eeyou Istchee Cree. In order to contribute to the documentation of the antidiabetic activities of 17 medicinal plants of the boreal forest traditionally recommended for treating the symptoms of diabetes, this study evaluates the pancreatic lipase enzymatic activity of different plant species. In addition, an evaluation of the enzymatic activity of the pancreatic lipase is carried out with antidiabetic species of the urban pharmacopoeia of Niamey (Niger) as well as with Quebec berries. Finally, phenolic compounds are identified in these last two groups of plant species. Results of these studies demonstrate that the majority of the evaluated species have an inhibitory effect on pancreatic lipase in vitro. Species showing the strongest inhibitory activities towards pancreatic lipase are Kalmia angustifolia, Gaultheria hispidula and Acacia nilotica. Thus, this study supports the accuracy of traditionnal knowledge by adding the documentation of an antidiabetic activity of plant species to the scientific repertoire.
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Book chapters on the topic "Pancreatic lipase inhibitor"

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Modanwal, Shristi, and Nidhi Mishra. "In Silico Analysis of Glucosinolates as Pancreatic Lipase Inhibitor to Develop Anti-obesity Drug." In Proceedings of the 2nd International Conference on Recent Trends in Machine Learning, IoT, Smart Cities and Applications, 409–18. Singapore: Springer Singapore, 2022. http://dx.doi.org/10.1007/978-981-16-6407-6_37.

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Sridhar, S. N. C., Ginson George, Aanchal Verma, and Atish Tulshiram Paul. "Natural Products-Based Pancreatic Lipase Inhibitors for Obesity Treatment." In Natural Bio-active Compounds, 149–91. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-7154-7_6.

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de Oliveira, Matheus Gabriel, Waléria Ramos Nogueira de Souza, Ricardo Pereira Rodrigues, Daniel F. Kawano, Leonardo Luiz Borges, and Vinicius Barreto da Silva. "Pharmacophore Mapping of Natural Products for Pancreatic Lipase Inhibition." In Emerging Research in Science and Engineering Based on Advanced Experimental and Computational Strategies, 305–38. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-31403-3_12.

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Patil, Samadhan, Mohini Patil, Vijay L. Maheshwari, and Ravindra H. Patil. "Pancreatic Lipase (PL) Inhibitors from Medicinal Plants and Their Potential Applications in the Management of Obesity." In Natural Products as Enzyme Inhibitors, 153–67. Singapore: Springer Nature Singapore, 2022. http://dx.doi.org/10.1007/978-981-19-0932-0_7.

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Gargouri, Y., G. Piéroni, C. Rivière, L. Sarda, and R. Verger. "Inhibition of Pancreatic and Microbial Lipases by Proteins: Kinetic and Binding Studies." In Enzymes of Lipid Metabolism II, 23–27. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5212-9_3.

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Cambillau, Christian, Yves Bourne, Marie Pierre Egloff, Chrislaine Martinez, and Herman van Tilbeurgh. "[5] Pancreatic lipases and their complexes with colipases and inhibitors: Crystallization and crystal packing." In Methods in Enzymology, 107–19. Elsevier, 1997. http://dx.doi.org/10.1016/s0076-6879(97)84007-4.

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Conference papers on the topic "Pancreatic lipase inhibitor"

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Subandi, Melly Wijaya, Tatas P. Broto Sudarmo, and Endang Suarsini. "Saponin isolates from cucumber (Cucumis sativus L.) fruit mesocarp and their activity as pancreatic lipase inhibitor." In THE 8TH ANNUAL BASIC SCIENCE INTERNATIONAL CONFERENCE: Coverage of Basic Sciences toward the World’s Sustainability Challanges. Author(s), 2018. http://dx.doi.org/10.1063/1.5062814.

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Sari, Harsiwi Candra, Sri Rahayu Lestari, Rina Rifqie Mariana, and Subandi Subandi. "In vitro and in silico analysis of cucumber (Cucumis sativus L.) mesocarp powder as pancreatic lipase and α-amylase inhibitor." In INTERNATIONAL CONFERENCE ON LIFE SCIENCES AND TECHNOLOGY (ICoLiST 2020). AIP Publishing, 2021. http://dx.doi.org/10.1063/5.0052669.

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Zhang, Tao, and Xingguo Wang. "Anti-obesity potential of 4,4-dimethylsterols by inhibiting pancreatic lipase." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/vixw6856.

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This study purified three classes of phytosterols from the unsaponifiable matter of different vegetable oils using preparative chromatography. Subsequently, their anti-obesity activity and lipase inhibitory activity were compared using in vivo mice model, in vitro digestion, and molecular docking. Results indicated that the 4,4-dimethylsterols displayed higher anti-obesity ability through promoting fecal triacylglycerol excretion and improving fatty acid profiles in adipose tissues. In contrast, the 4-demthylsteols showed higher cholesterol-lowering activity. In vitro digestion further proved the 4,4-dimethylsterols significantly decreased the hydrolysis activity of pancreatic lipase, achieving a higher fatty acid release than 4-desmethylsteorls. Finally, the inhibitory mechanism was proposed as that the 4,4-dimethylsterols possess a hydrogen-binding interaction with the Ser153 in the lipase catalytic pocket, presumably due to the polarity of hydroxyl group shielded by the two methyl groups in the structure. Overall, the present work concluded that the inhibitory activity on pancreatic lipase by 4,4-dimethylsterols can potentially ameliorate diet-induced obesity.
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Baba, Waqas, and Sajid Maqsood. "Novel antihypertensive and anticholesterolemic peptides from peptic hydrolysates of camel whey proteins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/qecs2081.

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Hypercholesterolemia and hypertension are major growing concerns that are managed by drugs that inhibit various metabolic enzymes. Milk hydrolysates have been reported to contain various bioactive peptides (BAP) that can inhibit various metabolic enzymes for enhancing human health. As such camel whey proteins were subjected to peptic hydrolysis using a full factorial model (33) with hydrolysis time, temperature, and enzyme concentration as factors. The resulting hydrolysates were analyzed for anti-hypercholesterolemic and hypertensive properties by studying the in vitro inhibition of various enzymatic markers. The hydrolysates with lowest IC50 values were further subjected to LC-MS-QTOF that revealed presence of 185 peptides. Selected peptides that had Peptide Ranker Score greater than 0.8 were further studied for prediction of possible interactions with enzyme markers: pancreatic lipase (PL) cholesterol esterase (CE) and angiotensin converting enzyme (ACE) using in silico analysis. The data generated suggested that most of the peptides could bind active site of PL while as only three peptides could bind active site of CE. Based on higher number of reactive residues in the bioactive peptides (BAP) and greater number of substrate binding sites, FCCLGPVPP was identified as potential CE inhibitory peptide while PAGNFLPPVAAAPVM, MLPLMLPFTMGY, and LRFPL were identified as PL inhibitors. While peptides PAGNFLP, FCCLGPVPP, PAGNFLMNGLMHR, PAVACCLPPLPCHM were identified as potential ACE inhibitors. Molecular docking of selected peptides showed hydrophilic and hydrophobic interactions between peptides and target enzymes. Moreover, due to the importance of renin in managing hypertension, peptides from hydrolysates with high ACE inhibiting potential were predicted for potential to interact with renin using in silico analysis. Molecular docking was subsequently employed to identify how the identified peptides, PVAAAPVM and LRPFL, could interact with renin and potentially inhibit it. Thus, non-bovine (camel) whey hydrolysates might be used as functional ingredients for production of functional foods with antihypertensive and anticholesterolemic properties.
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Shanker, Karuna, and Pooja Gaur. "HPLC based fractionation and microtiter plate-based bioactivity profiling of <em>Ocimum sanctum</em> Linn. leaves for potential pancreatic lipase inhibitor(s)." In 7th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/ecmc2021-11371.

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Buchholz, T., C. Görick, G. Wolber, and MF Melzig. "Pancreatic Lipase Inhibitors from Roselle – Natural Obesity Treatment." In GA 2017 – Book of Abstracts. Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1608159.

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Rufino, Ana, Maria Lobo, Silvia Rocha, Marco Zanchetta, Vera Silva, Artur Silva, and Eduarda Fernandes. "Evaluation of the anti-obesity potential of polyphenols through pancreatic lipase inhibition." In 7th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/ecmc2021-11401.

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Nguyen, Phuong, Dao Tran, and Han Huynh. "AURONE AS PROMISING HUMAN PANCREATIC LIPASE INHIBITORS THROUGH IN SILICO STUDY." In The 23rd International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2019. http://dx.doi.org/10.3390/ecsoc-23-06505.

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Tran, Thanh-Dao, Hoai-Anh Nguyen, Trong-Nhat Do, Van-Dat Truong, Khac-Minh Thai, and Ngoc-Chau Tran. "Design, Synthesis and Biological Evaluation of some Chalcone Derivatives as Potential Pancreatic Lipase Inhibitors." In The 17th International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2013. http://dx.doi.org/10.3390/ecsoc-17-b021.

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Tran, Dao. "Design, Synthesis and Biological Evaluation of some Chalcone Derivatives as Potential Pancreatic Lipase Inhibitors." In The 17th International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2013. http://dx.doi.org/10.3390/ecsoc-17-b024.

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