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Expression, purification and thermal stability evaluation of an engineered amaranth protein expressed in Escherichia coli Electron. J. Biotechnol.
Morales-Camacho,Jocksan I; Paredes-López,Octavio; Espinosa-Hernández,Edgar; Fernández Velasco,Daniel Alejandro; Luna-Suárez,Silvia.
Background: The acidic subunit of amarantin (AAC)-the predominant amaranth seed storage protein-has functional potential and its third variable region (VR) has been modified with antihypertensive peptides to improve this potential. Here, we modified the C-terminal in the fourth VR of AAC by inserting four VY antihypertensive peptides. This modified protein (AACM.4) was expressed in Escherichia coli. In addition, we also recombinantly expressed other derivatives of the amarantin protein. These include: unmodified amarantin acidic subunit (AAC); amarantin acidic subunit modified at the third VR with four VY peptides (AACM.3); and amarantin acidic subunit doubly modified, in the third VR with four VY peptides and in the fourth VR with the RIPP peptide...
Tipo: Journal article Palavras-chave: Globulin 11S; Protein expression; Protein engineering; Thermal stability.
Ano: 2016 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000400007
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Kinetic characterization of glucose aerodehydrogenase from Aspergillus niger EMS-150-F after optimizing the dose of mutagen for enhanced production of enzyme BJM
Umbreen,Huma; Zia,Muhammad Anjum; Rasul,Samreen.
In the present study enhanced production of glucose aerodehydrogenase from Aspergillus niger has been achieved after optimizing the dose of chemical mutagen ethyl methane sulfonate (EMS) that has not been reported earlier. Different doses of mutagen were applied and a strain was developed basing upon the best production. The selected strain Aspergillus niger EMS-150-F was optimized for nutrient requirements in order to produce enzyme through fermentation and the results showed the best yield at 2% corn steep liquor (CSL), 36 hours fermentation time, pH 5, 30°C temperature, 0.3% KH2PO4, 0.3% urea and 0.06% CaCO3. The enzyme was then purified and resulted in 57.88 fold purification with 52.12% recovery. On kinetic characterization, the enzyme showed optimum...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Glucose aerodehydogenase; Mutagenesis; Production; Purification; Thermal stability.
Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822013000400012
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PARTIAL CHARACTERIZATION OF PROTEASES FROM STREPTOMYCES CLAVULIGERUS USING AN INEXPENSIVE MEDIUM BJM
Moreira,Keila Aparecida; Cavalcanti,Maria Taciana Holanda; Duarte,Helena Simões; Tambourgi,Elias Basile; Melo,Eduardo Henrique Magalhães de; Silva,Valdinete Lins; Porto,Ana Lúcia Figueiredo; Lima Filho,José Luiz de.
The partial characterization of extracellular proteases from Streptomyces clavuligerus NRRL 3585 and 644 mutant was investigated. The enzyme production was carried out in batch fermentation using soy bean filtrate as nitrogen source. Maximum activity was obtained after 96h of fermentation with an initial pH of 7.0. The enzyme was partially purified by ammonium sulphate precipitation. Enzymes from the two strains retained 37% of their initial activities at pH 8.0 after 2 h incubation at 25ºC. Enzyme half-life at pH 8.0 and 60ºC was 40.30 and 53.32 min, respectively for both strains (partially purified extract). The optimum pH was obtained at pH 7.0-8.0 and 8.4 for enzymes produced for 3585 and 644 strains (crude extract), respectively, and 8.4 and 8.0 for...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Streptomyces clavuligerus; Extracellular proteases; Thermal stability; PH.
Ano: 2001 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822001000300010
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Purification and characterization of cytosolic and cell wall β-galactosidases from Vigna unguiculata stems Braz. J. Plant Physiol.
Sudério,Fabrício Bonfim; Barbosa,Gislainy Karla da Costa; Gomes-Filho,Enéas; Enéas-Filho,Joaquim.
Three β-galactosidase isoforms, β-gal I and β-gal II (cytosolic) and β-gal III (cell wall-associated), were isolated from stems of Vigna unguiculata (L.) Walp. cv. Pitiúba seedlings. Purification consisted of aμMonia sulfate fractionation followed by chromatography in DEAE-Sephadex and Lactosyl-Sepharose columns. The two cytosolic isoforms showed the same chromatography pattern, which differed from that of β-gal III. Electrophoresis revealed a single band of protein for β-gal II and β-gal III which also expressed β-galactosidase activity in gel. The apparent molecular mass of the β-gal I, II and III was 89, 146 and 124 kDa, respectively. The three isoforms revealed the same optimal pH (4.0) and the same optimal assay temperature (55ºC) for enzyme activity....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Enzymatic kinetics; Cowpea; Optimal pH; Enzyme purification; Thermal stability; Thermal inactivation.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202011000100003
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