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91 results for “lipases”
Development of an Amine Transaminase-Lipase Cascade for Chiral Amide Synthesis under Flow Conditions
<p>The use of multienzymatic systems has gained increasing attention as a method of choice for complex (asymmetric) syntheses. Incompatibilities between substrates, reagents and/or enzymes in one-pot batch conditions can hamper the applicability of a pursued cascade, so the use of flow systems provide useful synthetic solutions. The implementation of immobilised enzymes in continuous flow reactors allows the compartmentalisation and segregation of the enzymes in separate reactors, leading to otherwise disfavoured reaction cascades. Here, an amine transaminase and a lipase have been immobilised on polymer-coated controlled porosity glass carrier materials and studied for the first time together in the transamination of a prochiral ketone followed by acylation of the corresponding chiral amine in flow mode, two incompatible transformations under batch. Thus, the preparation of (<em>R</em>)-<em>N</em>-(1-phenoxypropan-2-yl)acetamide was accomplished after optimisation of the reaction conditions.</p>
Chemoselective Lipase-Catalyzed Synthesis of Amido Derivatives from 5-Hydroxymethylfurfurylamine
<p>The acylations of furfurylamine and 5-hydroxymethylfurfurylamine (HMFA) have been studied finding immobilized <i>Candida antarctica</i> lipase B (CALB) as an ideal biocatalyst. CALB was used immobilized on two different supports (Novozyme 435 and EziG-CALB), with the polymer-coated controlled porosity glass carrier material from EnginZyme being an excellent carrier to yield an active and stable enzymatic preparation for the acylation of the primary amine group. The amount of the acyl donor in the reaction was a key factor to achieve the mono- and chemoselective N-protection of HMFA with large excess of ethyl acetate leading to the formation of the N,O-diacetylated product. Thus, a series of 16 nonactivated esters were used to selectively modify the amine group of HMFA, obtaining 9 hydroxy amides under mild reaction conditions and with quantitative yields through chromatography-free transformations. The influence of substrate concentration was studied, resulting in complete conversions in all cases after 22 h (100–1000 mM). Excellent results were observed at 100 and 200 mM of HMFA, while higher concentrations led to longer reaction times and, to some extent, the formation of the diacetylated product (up to 7% after 22 h at 1 M). After this optimization, a metric analysis was performed to confirm the high sustainability of the presented process (<i>E</i>-factor of 1.1 excluding solvents) upon intensification of the biotransformation to 1 g at 200 mM HMFA concentration. The possibility of obtaining orthogonally protected HMFA-derived amido esters has been achieved through a clean and sequential one-pot process using EziG-CALB, which involved the use of ethyl methoxy acetate as the nonactivated ester for N-acylation and the activated vinyl acetate for O-protection.</p>
Structure and Mechanism of a Cold-Adapted Bacterial Lipase
<p>Input files and structures used to obtain computational results published in:</p> <p><a href="https://doi.org/10.1021/acs.biochem.2c00087?urlappend=%3Fref%3DPDF&jav=AM&rel=cite-as">Structure and Mechanism of a Cold-Adapted Bacterial Lipase</a><br> DOI: 10.1021/acs.biochem.2c00087</p> <p>See included README file and publication for more details.</p> <p>Funding<br> This work was supported by the Swedish Research Council<br> (VR), the Knut and Alice Wallenberg Foundation, and the<br> Research Council of Norway through a Centre of Excellence<br> and project grant (Grant Nos. 262695 and 274858).<br> Computational resources were provided by the Swedish<br> National Infrastructure for Computing (SNIC)</p>
Figure 7 in Supported ionic liquid phase facilitated catalysis with lipase from Aspergillus oryzae for enhance enantiomeric resolution of racemic ibuprofen - NCN project OPUS, grant no. 2020/37/B/ST8/00693.
<p>Figure 7. presents the scheme of ionic liquid immobilization on the silica surface. The file relates to the composite material manufactured for the NCN project OPUS, grant no. 2020/37/B/ST8/00693.</p>
Safety, Tolerability, Efficacy, Pharmacokinetics, and Pharmacodynamics of Sebelipase Alfa in Children With Growth Failure Due to Lysosomal Acid Lipase Deficiency
ClinicalTrials.gov study NCT01371825. IPD Sharing: UNDECIDED. Countries: 5. Publications: 1.
Extension Study to Evaluate the Long-Term Safety, Tolerability, and Efficacy of SBC-102 (Sebelipase Alfa) in Adult Subjects With Lysosomal Acid Lipase Deficiency
ClinicalTrials.gov study NCT01488097. IPD Sharing: Not stated. Countries: 5. Publications: 2.
Safety, Tolerability and Pharmacokinetics of SBC-102 (Sebelipase Alfa) in Adult Participants With Lysosomal Acid Lipase Deficiency
ClinicalTrials.gov study NCT01307098. IPD Sharing: UNDECIDED. Countries: 4. Publications: 1.
First in Human Study of a Monoclonal Antibody (SOL-116) Targeting BSSL (Bile Salt-Stimulated Lipase), Single and Multiple Dose Parts
ClinicalTrials.gov study NCT05576012. IPD Sharing: NO. Countries: 1. Publications: 0.
Clinical Study In Infants With Rapidly Progressive Lysosomal Acid Lipase Deficiency
ClinicalTrials.gov study NCT02193867. IPD Sharing: Not stated. Countries: 4. Publications: 3.
Acid Lipase Replacement Investigating Safety and Efficacy (ARISE) in Participants With Lysosomal Acid Lipase Deficiency
ClinicalTrials.gov study NCT01757184. IPD Sharing: Not stated. Countries: 15. Publications: 4.
Safety and Efficacy Study of Sebelipase Alfa in Participants With Lysosomal Acid Lipase Deficiency
ClinicalTrials.gov study NCT02112994. IPD Sharing: Not stated. Countries: 15. Publications: 1.
Protein preparation (1LPB), docked structures of Bromhexine and Orlistat to Pancreatic Lipase, and MD simulations trajectories in 3 replicas.
<p>Data set contains 3 folders:</p> <p>1) Protein preparation (1LPB)</p> <p>2) XP Docking of Bromhexine and Orlistat</p> <p>3) MD Simulation of Bromhexine and Orlistat (3 replicates)</p>
Fig. 5 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives
Fig. 5. Docking of compounds 3, 9, 11 and 15 in human lipase. The structure of lipase (green surface) with the residues lining the binding pocket (sticks with white carbons) and the catalytic resides (S169, D193 and H280 in yellow). The docking results in lipase with compounds 3 (pink, A), 9 (cyan, B), 11 (magenta, C) and 15 (green, D) are shown with their main interacting residues labelled, hydrogen bonds and binding energies. (E) Zoom in on the superimposition of the docked compounds 3, 9, 11 and 15 (coloured as in A-D) with the position of the aromatic rings encircled and the residues, which interact with all compounds of them, are labelled. (F) The original structure of lipase (1LPB) contains the inhibitor methoxy-undecylphosphinic acid (MUP in purple). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 2 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives
Fig. 2. In vitro inhibition activities.α-Amylase inhibition (A) andα-glucosidase inhibition (B) by acarbose and the pure active compounds. (C) Pancreatic lipase inhibition by orlistat and the pure active compounds. In each test, data are expressed as IC50 values in μM and values with the same letter (a–h) are not significantly different at p ≤ 0.05 level, according to a one-way analysis of variance (ANOVA).
Fig. 4 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives
Fig. 4. Docking of compounds 3, 9, 11, and 15 in human lipase enzyme. The original structure of the lipase enzyme (1LPB) contains the inhibitor methoxyundecylphosphinic acid (MUP, carbons coloured purple (A)). The docking results in lipase enzyme (B-E, green surface) with compounds 3 (pink, B), 9 (cyan, C), 11 (magenta, D), and 15 (green, E) are shown with their respective binding energies. The carbons of the residues lining the binding pocket are coloured in white, with the active site residues in yellow (S169, D193, and H280). Residues making hydrogen bonds with the ligands are indicated (B–E). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 3 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives
Fig. 3. Docking of compounds 3, 9, 11, and 15 in human α-amylase and α-glucosidase enzymes. The original structures of α-amylase (1XD0) and α-glucosidase (3TOP) enzymes contain the inhibitor acarbose (carbons coloured in orange and hexoses numbered in A and F, respectively). The docking results in α-amylase (B-E, light grey surface) and α-glucosidase (G-J, beige) enzymes with compounds 3 (pink, B and G), 9 (cyan, C and H), 11 (magenta, D and I), and 15 (green, E and J) are shown with their respective binding energies. The carbons of the residues lining the binding pocket are coloured in white, with the active site residues in yellow (R210, D212, E248, and R352 in α-amylase; D1420, E1423, and D1526 in α-glucosidase enzyme). Residues making hydrogen bonds with the ligands are indicated (B- E and G-J). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 6 in Mobilization of storage lipid reserve and expression analysis of lipase and lipoxygenase genes in rice (Oryza sativa var. Pusa Basmati 1) bran during germination
Fig. 6. Expression analysis of rice bran lipase genes using quantitative RT PCR (qRT PCR) during 2 HAI, 1, 2, 4, 6, and 8 DAI. Expression value at 0 HAI was taken as control while elongation factor 1-alpha (EF1A, accession no.: XM_015774317.2) was used as the reference gene to normalize the expression level of lipases used in this study. Bars represent means ± standard deviation (SD) of 3 biological replicates. HAI, hours after imbibition; DAI, days after imbibition.
Fig. 5 in Mobilization of storage lipid reserve and expression analysis of lipase and lipoxygenase genes in rice (Oryza sativa var. Pusa Basmati 1) bran during germination
Fig. 5. Schematic representation of the conserved motifs in (a) OsLip proteins and (b) OsLOX proteins. Each colored box represents a motif in the respective protein sequence. Motif number and color codes indicate the sequence of the conserved motif. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 1 in Mobilization of storage lipid reserve and expression analysis of lipase and lipoxygenase genes in rice (Oryza sativa var. Pusa Basmati 1) bran during germination
Fig. 1. Lipid and FA content in bran of germinating rice grains. (a) Lipid content in bran tissues (b) FA profiles of TAGs (c) FA profiles of DAGs (d) FA profiles of NEFAs and (e) FA profiles of PLs. TAG, Triacylglycerol; DAG, diacylglycerol; NEFA, non-esterified fatty acid; PL, polar lipid. Results are mean values ± SD of three replicates.
Fig. 7 in Mobilization of storage lipid reserve and expression analysis of lipase and lipoxygenase genes in rice (Oryza sativa var. Pusa Basmati 1) bran during germination
Fig. 7. Expression analysis of rice bran LOX genes using quantitative RT PCR (qRT PCR) during 2 HAI, 1, 2, 4, 6, and 8 DAI. Expression value at 0 HAI was taken as control while elongation factor 1-alpha (EF1A, accession no.: XM_015774317.2) was used as the reference gene to normalize the expression level of LOXs used in this study. Bars represent means ± standard deviation (SD) of 3 biological replicates. HAI, hours after imbibition; DAI, days after imbibition.
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