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	Provedor de dados Electron. J. Biotechnol. (2) J. Venom. Anim. Toxins incl. Trop. Dis. (2) BJM (1) Autor Amorim,Fernanda G. (1) Arantes,Eliane C. (1) Astofi-Filho,Spartaco (1) Bordon,Karla C F (1) Bressan,W. (1) Cavalett,Angélica (1) Chen,Fang (1) Figueiredo,J. E. F. (1) Gomez,M. V. (1) Hu,Xiaole (1) Kalapothakis,E. (1) Kipnis,André (1) Lima,André O.S (1) Rodrigues,André L (1) Torres,Fernando Araripe Gonçalves (1) Wei,Lei (1) Wiezel,Gisele A. (1) Xavier,Mauro Aparecido Souza (1) Xu,Ying (1) Yin,Li (1) Mais... Palavra-chave Heterologous expression (5) Escherichia coli (2) Molecular cloning (2) Beta-glucosidase (1) Bioinsecticide (1) Biotechnological applications (1) Caterpillar (1) Cellulase cassette (1) Cellulose bioconversion (1) Cloning (1) Endoglucanase (1) Hyaluronidase (1) Hymenoptera (1) Induced expression (1) Insects (1) PEGylation (1) Scorpion (1) Southern blot (1) Spider (1) Spodoptera frugiperda (1) Mais... Tipo do documento Info:eu-repo/semantics/article (3) Journal article (2) Ano 2015 (1) 2014 (1) 2010 (1) 2009 (1) 2008 (1) País Brazil (3) Chile (2) Idioma Inglês (5)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 5 Primeira ... 1 ... Última 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 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 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 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 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 Registros recuperados: 5 Primeira ... 1 ... Última

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