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Registros recuperados: 3
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Exploring the active site cavity of human pancreatic lipase Inra
Colin, D.Y.; Deprez-Beauclair, P.; Allouche, M.; Brasseur, R.; Kerfelec, B..
Within the scope of improving the efficiency of pancreatic enzyme replacement therapy in cystic fibrosis, the feasibility of shifting the pH-activity profile of pancreatic lipase toward acidic values was investigated by site specific mutagenesis in different regions of the catalytic cavity. We have shown that introducing a negative charge close to the catalytic histidine induced a shift of the pH optimum toward acidic values but strongly reduced the lipase activity. On the other hand, a negative charge in the entrance of the catalytic cleft gives rise to a lipase with improved properties and twice more active than the native enzyme at acidic pH
Tipo: Journal Article Palavras-chave: DUODENUM; MUCOVISCIDOSE; ACIDITE PANCREATIC LIPASE; CYSTIC FIBROSIS; PH ACTIVITY PROFILE; COLIPASE.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008b28a35bf&uri=/notices/prodinra1/2008/06/
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Modification of pancreatic lipase properties by directed molecular evolution Inra
Colin, D.; Deprez, P.; Silva, N.; Infantes, L.; Kerfelec, B..
Cystic fibrosis is associated with pancreatic insufficiency and acidic intraluminal conditions that limit the action of pancreatic enzyme replacement therapy, especially that of lipase. Directed evolution combined with rational design was used in the aim of improving the performances of the human pancreatic lipase at acidic pH. We set up a method for screening thousands of lipase variants for activity at low pH. A single round of random mutagenesis yielded one lipase variant with an activity at acidic pH enhanced by ∼50% on medium- and long-chain triglycerides. Sequence analysis revealed two substitutions (E179G/N406S) located in specific regions, the hydrophobic groove accommodating the sn-1 chain of the triglyceride (E179G) and the surface loop that is...
Tipo: Journal Article Palavras-chave: ACTIVITE ENZYMATIQUE COLIPASE; CYSTIC FIBROSIS; DIRECTED EVOLUTION; PANCREATIC LIPASE; SUBSTRATE SPECIFICITY; TRIGLYCERIDES.
Ano: 2010 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2011f8ff0194&uri=/notices/prodinra1/2011/06/
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Structure and orientation of pancreatic colipase in a lipid environment: PM-IRRAS and Brewster Angle Microscopy studies Inra
Allouche, M.; Castano, S.; Colin, D.; Desbat, B.; Kerfelec, B..
Colipase is a key element in lipase-catalyzed dietary lipids hydrolysis. Although devoid of enzymatic activity, colipase promotes pancreatic lipase activity in the physiological intestinal conditions by anchoring the enzyme on the surface of lipid droplets. Polarization modulation infrared reflection absorption spectroscopy combined with Brewster angle microscopy studies was performed on colipase alone and in various lipid environments to obtain a global view of both conformation and orientation and to assess lipid perturbations. We clearly show that colipase fully inserts into a dilaurin monolayer and promotes the formation of lipid/protein domains, whereas in a phospholipid environment its insertion is only partial, limited to the polar head group. In a...
Tipo: Journal Article Palavras-chave: ACTIVITE ENZYMATIQUE; PANCREAS; SPECTROSCOPIE PM-IRRAS; COLIPASE.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20085218fbca&uri=/notices/prodinra1/2008/01/
Registros recuperados: 3
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