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Combined mass mapping and biochemical characterization of grape beta-glycosidase-enriched extract Inra
Sarry, J.E.; Grimplet, J.; Sommerer, N.; Vallier, M.J.; Pradal, M.; Mondolot, L.; Andary, C.; Gunata, Z.; Romieu, C..
A beta-glucosidase enzyme activity was enriched from skins of ripe grape berry by cell wall fractionation, hydrophobic interaction and cation-exchange chromatographies. This enriched enzyme extract contained several beta-glycosidase activities hydrolyzing a wide range of synthetic and natural monoglycosides and diglycosides, as well as a beta-fructosidase activity. The enzyme extract was further characterized by two-dimensional gel electrophoresis coupled to peptide mass fingerprinting of eight spots using MALDI-TOF mass spectrometry. No beta-glucosidase but a beta-fructosidase associated to the relevant spot at 66 kDa/pI 5.1 was identified. Taken together all results issued from the biochemical characterization, the substrate specificity and the mass...
Tipo: Journal Article Palavras-chave: BETA-GLYCOSIDASE; MASS MAPPING; SUBSTRATE SPECIFICITY; PROTEOME; GRAPE.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008c84ba3d7&uri=/notices/prodinra1/2009/02/
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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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