Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 3
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Complete hydrolysis of myo-inositol hexakisphosphate by a novel phytase from Debaryomyces castellii CBS 2923 Inra
Ragon, M.; Aumelas, A.; Chemardin, P.; Galvez, S.; Moulin, G.; Boze, H..
Debaryomyces castellii phytase was purified to homogeneity in a single step by hydrophobic interaction chromatography. Its molecular mass is 74 kDa with 28.8% glycosylation. Its activity was optimal at 60 C and pH 4.0. The Km value for sodium phytate was 0.532 mM. The enzyme exhibited a low specificity and hydrolyzed many phosphate esters. The phytase fully hydrolyzed myo-inositol hexakisphosphate ( or phytic acid, Ins P-6) to inositol and inorganic phosphate. The sequence of Ins P-6 hydrolysis was determined by combining results from high-performance ionic chromatography and nuclear magnetic resonance. D. castellii phytase is a 3-phytase that sequentially releases phosphate groups through Ins ( 1,2,4,5,6) P-5, Ins ( 1,2,5,6) P-4, Ins ( 1,2,6) P-3, Ins (...
Tipo: Journal Article Palavras-chave: DEBAROMYCES CASTELLII; YEAST; PHYTASE; ENZYME CHARACTERIZATION; INOSITOL PHOSPHATE; PHYTATE DEGRADATION; NMR; HPLC.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009150d6498&uri=/notices/prodinra1/2010/09/
Imagem não selecionada

Imprime registro no formato completo
Molecular gene cloning and overexpression of the phytase from Debaryomyees castellii CBS 2923 Inra
Ragon, M.; Neugnot-Roux, V.; Chemardin, P.; Moulin, G.; Boze, H..
The ORF encoding the Debaryomyces castellii CBS 2923 phytase was isolated. The deduced 461-amino-acid sequence corresponded to a 51.2 kDa protein and contained the consensus motif (RHGXRXP) which is conserved among phytases. No signal sequence cleavage site was detected. Nine potential N-glycosylation sites have been predicted. The protein shared 21-69% sequence identities with various phytases of yeast or fungal origin. Heterologous expression of the D. castellii CBS 2923 phytase in the methylotrophic yeast Pichia pastoris was tested under both the P. pastoris inducible alcohol oxidase (AOX1) promoter and the constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. Maximum production levels obtained were 476 U ml(-1), with the AOX1 expression...
Tipo: Journal Article Palavras-chave: GENE ISOLATION; PHYTASE; DEBARYOMYCES CASTELLII; PICHIA PASTORIS; HETEROLOGOUS EXPRESSION.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009ea2756c4&uri=/notices/prodinra1/2010/08/
Imagem não selecionada

Imprime registro no formato completo
NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: model of the possible lipid A-binding site Inra
Yang, Y.; Boze, H.; Chemardin, P.; Padilla, A.; Moulin, G.; Tassanakajon, A.; Pugnière, M.; Roquet, F.; Destoumieux-Garzon, D.; Gueguen, Y.; Bachère, E.; Aumelas, A..
The anti-lipopolysaccharide factor ALF-Pm3 is a 98-residue protein identified in hemocytes from the black tiger shrimp Penaeus monodon. It was expressed in Pichia pastoris from the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter as a folded and N-15 uniformly labeled rALF-Pm3 protein. Its 3D structure was established by NMR and consists of three alpha-helices packed against a four-stranded beta-sheet. The C-34-C-55 disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that rALF-Pm3 binds to LPS, lipid A and to OM(R)-174, a soluble analogue of lipid A. Biophysical studies of rALF-Pm3/LPS and rALF-Pm3/OM(R)-174 complexes indicated rather high molecular sized aggregates, which...
Tipo: Journal Article Palavras-chave: ANTI-LIPOPOLYSACCHARIDE FACTOR ; LIPOPOLYSACCHARIDE; LIPID A; NMR; STRUCTURE; SEPTIC SHOCK; SURFACE PLASMON RESONANCE ULTRACENTRIFUGATION.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD201064bb8a78&uri=/notices/prodinra1/2010/09/
Registros recuperados: 3
Primeira ... 1 ... Última
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional