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Registros recuperados: 9
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A novel chloroplastic isopentenyl diphosphate isomerase gene from Jatropha curcas: Cloning, characterization and subcellular localization Electron. J. Biotechnol.
Wei,Lei; Yin,Li; Hu,Xiaole; Xu,Ying; Chen,Fang.
Background Jatropha curcas is a rich reservoir of pharmaceutically active terpenoids. More than 25 terpenoids have been isolated from this plant, and their activities are anti-bacterial, anti-fungal, anti-cancer, insecticidal, rodenticidal, cytotoxic and molluscicidal. But not much is known about the pathway involved in the biosynthesis of terpenoids. The present investigation describes the cloning, characterization and subcellular localization of isopentenyl diphosphate isomerase (IPI) gene from J. curcas. IPI is one of the rate limiting enzymes in the biosynthesis of terpenoids, catalyzing the crucial interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Results A full-length JcIPI cDNA consisting of 1355 bp was cloned....
Tipo: Journal article Palavras-chave: Heterologous expression; Southern blot; Terpenoids; Transient expression.
Ano: 2014 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000600007
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Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology J. Venom. Anim. Toxins incl. Trop. Dis.
Bordon,Karla C F; Wiezel,Gisele A.; Amorim,Fernanda G.; Arantes,Eliane C..
AbstractHyaluronidases are enzymes that mainly degrade hyaluronan, the major glycosaminoglycan of the interstitial matrix. They are involved in several pathological and physiological activities including fertilization, wound healing, embryogenesis, angiogenesis, diffusion of toxins and drugs, metastasis, pneumonia, sepsis, bacteremia, meningitis, inflammation and allergy, among others. Hyaluronidases are widely distributed in nature and the enzymes from mammalian spermatozoa, lysosomes and animal venoms belong to the subclass EC 3.2.1.35. To date, only five three-dimensional structures for arthropod venom hyaluronidases (Apis mellifera and Vespula vulgaris) were determined. Additionally, there are four molecular models for hyaluronidases fromMesobuthus...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Hyaluronidase; Scorpion; Spider; Caterpillar; Hymenoptera; Insects; Cloning; Heterologous expression; PEGylation; Biotechnological applications.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100214
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Cloning and expression analysis of glucanase genes from Phytophthora cinnamomi IPB - Escola Superior Agrária
Martins, Ivone; Meirinho, Sofia; Dias, Teresa; Jorge, Lurdes; Martins, Fátima; Choupina, Altino.
Phytophthora cinnamomi is one among the most destructive species of Phytophthora associated to the decline of forestry, ornamental and fruit species. Associated with this oomycete is the ink disease of Castanea sativa Mill. Glucan endo-1,3-β-D-glucosidase catalyzes the hydrolysis of 1,3-β-D-glucoside linkages in callose, laminarin and several carbohydrates found in the cell wall of plants and fungi. It is generally thought that glucanases play a role in plant defence by digesting wall components of the fungal pathogen. In oomycetes, glucanases have been studied at biochemical level for their possible role in hyphal tip growth and branching, where there is thought to be a delicate balance between the cell wall synthesis and hydrolysis. Fungal cell wall...
Tipo: ConferenceObject Palavras-chave: Castanea sativa Mill; ENDO1; Homologous expression; Heterologous expression.
Ano: 2010 URL: http://hdl.handle.net/10198/3369
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Cloning, molecular characterization and heterologous expression of AMY1, an alfa-amylase gene from Cryptococcus flavus. Repositório Alice
GALDINO, A. S.; ULHOA, C. J.; MORAES, L. M. P.; PRATES, M. V.; BLOCH JÚNIOR, C.; TORRES, F. A. G..
Tipo: Separatas Palavras-chave: Cryptococcus flavus; Heterologous expression; Alfa-amylase; Saccharomyces Cerevisiae.
Ano: 2008 URL: http://www.alice.cnptia.embrapa.br/alice/handle/doc/190346
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Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes Electron. J. Biotechnol.
Rodrigues,André L; Cavalett,Angélica; Lima,André O.S.
Cellulase is a group of enzymes (endoglucanase, exoglucanase and beta-glucosidase) required for cellulosic feedstock hydrolysis during bioethanol production. The use of recombinant cellulase is a strategy to reduce the enzyme cost. In this context, the present work describes the construction of a cellulase expression vector (pEglABglA), which allowed constitutive co-expression of endoglucanase A (EglA) from an endophytic Bacillus pumilus and the hyperthermophilic β-glucosidase A (BglA) from Fervidobacterium sp. in Escherichia coli. When compared to the non-modified strain DH5α, the recombinant Escherichia coli DH5α (pEglABglA) reduced fivefold the viscosity of the carboxymethylcellulose medium (CMC-M). Also, it presented almost...
Tipo: Journal article Palavras-chave: Beta-glucosidase; Cellulase cassette; Cellulose bioconversion; Endoglucanase; Heterologous expression.
Ano: 2010 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000500005
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Expression in Escherichia coli and characterization of beta-xylosidases GH-39 and GH-43 from Bacillus halodurans C-125 Inra
Smaali, I.; Remond-Zilliox, C.; O Donohue, M..
To develop xylosidases as tools for the hydrolysis of wheat bran arabinoxylans, two beta-xylosidases from Bacillus halodurans C-125 have been cloned and expressed in Escherichia coli. The recombinant (His)6-tagged enzymes, designated as XylBH39 and XylBH43, were efficiently purified using Ni2+-affinity chromatography. Determination of native molecular masses indicated that XylBH43 is dimeric in solution, whereas a similar analysis of XylBH39 did not allow differentiation between the dimeric and trimeric states. Both enzymes had similar pH and temperature optima (pH 7.5 and 55°C for XylBH39 and pH 8 and 60°C for XylBH43) and were relatively stable over the pH range of 3.5–8.5. In contrast, XylBH39 was more thermostable. At 60°C, XylBH39 and XylBH43...
Tipo: Journal Article Palavras-chave: Xylosidase; Heterologous expression; Hemicelluloses; Bioconversion; Bacillus halodurans C-125.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20075d4d976a&uri=/notices/prodinra1/2010/09/
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Heterologous expression of an insecticidal gene from the armed spider (Phoneutria nigriventer) J. Venom. Anim. Toxins incl. Trop. Dis.
Figueiredo,J. E. F.; Kalapothakis,E.; Gomez,M. V.; Bressan,W..
Insect-pests are global problems that cause severe damage to crop plants, and their control is commonly based on chemical insecticides. However, negative effects of pesticides on the environment and human health emphasize the necessity to develop alternative methods for insect-pest control. In the present study, a gene coding for the insecticidal peptide TX4(6-1) of the Brazilian armed spider (Phoneutria nigriventer) was cloned in fusion with maltose binding protein (MBP) and expressed in Escherichia coli. The affinity purified protein MBP-GlyTX4 was cleaved with the Xa factor and used for a bioassay against Spodoptera frugiperda and rabbit immunization. Five micrograms GlyTX4 protein injected into the hemocoel of larvae and abdominal cavity of adults...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bioinsecticide; Molecular cloning; Heterologous expression; Escherichia coli; Spodoptera frugiperda.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992008000200006
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New vectors derives from pUC 18 for clonig and thermal-induced expression in Escherichia coli BJM
Xavier,Mauro Aparecido Souza; Kipnis,André; Torres,Fernando Araripe Gonçalves; Astofi-Filho,Spartaco.
We report the construction of two vectors for Escherichia coli: pUC72, for molecular cloning, and pPLT7, for thermal-induced expression. The main feature of pUC72 is a novel polylinker region that includes restriction sites for Nde I and Nco I which provide an ATG codon for proper translation initiation of expressed genes. Vector pPLT7 is ideal for thermo-inducible expression in host cells that carry the cI857 repressor gene. The use of pPLT7 was validated by the successful expression of the genes encoding carp and porcine growth hormones. These vectors provide novel cloning possibilities in addition to simple, non-expensive, high level expression of recombinant proteins in E. coli.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Heterologous expression; Escherichia coli; Molecular cloning; Induced expression.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000400007
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Optimization of inside and outside factors to improve recombinant protein yield in plant. Repositório Alice
HABIBI, P.; PRADO, G. S.; PELEGRINI, P. B.; HEFFERON, K. L.; SOCCOL, C. R.; GROSSI-DE-SA, M. F..
Tipo: Separatas Palavras-chave: Heterologous expression; Host systems; Post-translational modifications; Plant-based pharmaceuticals; Recombinant proteins.
Ano: 2017 URL: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1080464
Registros recuperados: 9
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