Results 11 to 20 of about 143,826 (243)

Characterization of a Plastid Triacylglycerol Lipase from Arabidopsis [PDF]

Plant Physiology, 2007
Full-length cDNA corresponding to Arabidopsis (Arabidopsis thaliana) gene At2g31690, which has been annotated in GenBank as a putative triacylglycerol (TAG) lipase, was obtained by reverse transcription-polymerase chain reaction using RNA from senescing ...
Anita K. Padham, Marianne T Hopkins, Tzann‐Wei Wang, Linda McNamara, Maisie Lo, Lynn G.L. Richardson, Matthew D. Smith, Catherine A. Taylor, John E. Thompson   +8 more
semanticscholar   +6 more sources

DAGL-Beta Functions as a PUFA-Specific Triacylglycerol Lipase in Macrophages. [PDF]

Cell Chem Biol, 2020
Here, we apply quantitative chemical proteomics and untargeted lipidomics to assign a polyunsaturated fatty acid (PUFA)-specific triacylglycerol (TAG) lipase activity for diacylglycerol lipase-beta (DAGLβ) in macrophages.
Shin M, Ware TB, Hsu KL.
europepmc   +2 more sources

Safety evaluation of the food enzyme triacylglycerol lipase from the non‐genetically modified Aspergillus luchuensis strain AE‐L [PDF]

EFSA Journal, 2023
The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase; EC 3.1.1.3) is produced with the non‐genetically modified Aspergillus luchuensis strain AE‐L by Amano Enzyme Inc. The food enzyme is free from viable cells of the production organism.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Vittorio Silano, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Lieve Herman, Ana Gomes, Magdalena Andryszkiewicz, Natalia Kovalkovicova, Yi Liu, Andrew Chesson   +22 more
doaj   +2 more sources

Safety evaluation of the food enzyme triacylglycerol lipase from the genetically modified Aspergillus luchuensis strain FL108SC [PDF]

EFSA Journal, 2023
The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase; EC 3.1.1.3) is produced with the genetically modified Aspergillus luchuensis strain FL108SC by Advanced Enzyme Technologies Ltd.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Lieve Herman, Yrjö Roos, Magdalena Andryszkiewicz, Ana Gomes, Natalia Kovalkovicova, Yi Liu, Andrew Chesson   +23 more
doaj   +2 more sources

Safety evaluation of the food enzyme triacylglycerol lipase from the genetically modified Saccharomyces cerevisiae strain LALL‐LI [PDF]

EFSA Journal, 2023
The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) is produced with the genetically modified Saccharomyces cerevisiae strain LALL‐LI by Lallemand Inc. The genetic modifications do not give rise to safety concerns. The food
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Yrjö Roos, Jaime Aguilera, Magdalena Andryszkiewicz, Yi Liu, Andrew Chesson   +21 more
doaj   +2 more sources

Soybean (Glycine max L.) triacylglycerol lipase GmSDP1 regulates the quality and quantity of seed oil. [PDF]

Sci Rep, 2019
Seeds of soybean (Glycine max L.) are a major source of plant-derived oils. In the past, improvements have been made in the quantity and quality of seed oil.
Kanai M, Yamada T, Hayashi M, Mano S, Nishimura M.   +4 more
europepmc   +2 more sources

Characterization of the putative yeast mitochondrial triacylglycerol lipase Tgl2. [PDF]

J Biol Chem
Mitochondria derive the majority of their lipids from other organelles through contact sites. These lipids, primarily phosphoglycerolipids, are the main components of mitochondrial membranes. In the cell, neutral lipids like triacylglycerides (TAGs) are stored in lipid droplets, playing an important role in maintaining cellular health.
Tiku V, Fakih Z, Tatsuta T, Jung M, Rapaport D, Dimmer KS.   +5 more
europepmc   +4 more sources

Cloning and sequencing of the triacylglycerol lipase gene of Aspergillus oryzae and its expression in Escherichia coli [PDF]

FEMS Microbiology Letters, 2000
Aspergillus oryzae produces at least three extracellular lipolytic enzymes, L1, L2 and L3 (cutinase, mono- and diacylglycerol lipase, and triacylglycerol lipase, respectively).
Jinichi Toida
semanticscholar   +3 more sources

Safety evaluation of the food enzyme triacylglycerol lipase from the genetically modified Aspergillus luchuensis strain FL100SC [PDF]

EFSA Journal, 2021
The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase EC 3.1.1.3) is produced with a genetically modified Aspergillus luchuensis strain FL100SC by Advanced Enzyme Technologies Ltd.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Lieve Herman, Magdalena Andryszkiewicz, Giovanni Bernasconi, Ana Gomes, Natalia Kovalkovicova, Yi Liu, Joaquim Maia, Sandra Rainieri, Andrew Chesson   +25 more
doaj   +2 more sources

Regulation of the yeast triacylglycerol lipase TGl3p by formation of nonpolar lipids. [PDF]

J Biol Chem, 2013
Background: Tgl3p from yeast serves as the major triacylglycerol lipase but also as lysophospholipid acyltransferase. Results: Formation of nonpolar lipids strongly affects subcellular localization and function of Tgl3p.
Schmidt C, Athenstaedt K, Koch B, Ploier B, Daum G.   +4 more
europepmc   +2 more sources