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Effect of temperature on polyunsaturated fatty acid accumulation in soybean seeds Braz. J. Plant Physiol.
Lanna,Anna Cristina; José,Inês Chamel; Oliveira,Maria Goreti de Almeida; Barros,Everaldo Gonçalves; Moreira,Maurilio Alves.
Soybean oil contains around 60 % of polyunsaturated fatty acids, which are responsible for the low oxidative stability of soy-derived products. Soybean lines with low linolenic acid content can be obtained by genetic manipulation; however, a high proportion of the variation in fatty acids content is due to environmental factors. This work aimed to determine the effect of temperature on oil composition and on the activity of the enzymes CDP-choline:1,2-diacylglycerolcholine phosphotransferase (CPT) and acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT), responsible for maintenance of polyunsaturated fatty acids in the cytoplasmic acyl-CoA pool, that is used for oil synthesis in the seeds. CAC-1, a soybean variety with linolenic acid content of about 8...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Cholinephosphotransferase; Kinetic characterization; Linoleic acid; Linolenic acid; Lysophosphatidylcholine acyltransferase; Soybean seed.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202005000200004
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Isolation and characterization of a newly isolated Pseudomonas mutant for protease production BABT
Dutta,Jayati Ray; Banerjee,Rintu.
A potent bacterium for extracellular protease production was isolated from local soil and identified as Pseudomonas sp. RAJR 044. A mutant of this strain JNGR 242 with protease productivity 2.5 fold higher was obtained by ultraviolet irradiation under experimentally optimized conditions of pH 7.0, temperature of 34ºC, inoculum volume of 1.0 mL and incubation time of 24 hours. Comparative analysis of the chemical characteristics i.e. assimilation of carbon and nitrogen sources were also carried out. Maximum growth of the mutant strain in 2% gelatin agar plate was obtained in presence of dextrose (2%), maltose (2%), ammonium sulfate (2%) and potassium nitrate (2%) whereas, that of the parent strain was found in sucrose (2%) and ammonium nitrate (2%). The...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Extracellular protease; Purification; Kinetic characterization; Ultraviolet mutagenesis; Pseudomonas sp.; Physicochemical.
Ano: 2006 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132006000100005
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Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa Anais da ABC (AABC)
Sena,Amanda R.; Júnior,Gildomar L.V.; Góes Neto,Aristóteles; Taranto,Alex G.; Pirovani,Carlos P.; Cascardo,Júlio C.M.; Zingali,Russolina B.; Bezerra,Marcos A.; Assis,Sandra A..
The enzyme glucanase from Moniliophthora perniciosa was produced in liquid medium and purified from the culture supernatant. A multivariate statistical approach (Response Surface Methodology - RSM) was employed to evaluate the effect of variables, including inducer (yeast extract) and fermentation time, on secreted glucanase activities M. perniciosa detected in the culture medium. The crude enzyme present in the supernatant was purified in two steps: precipitation with ammonium sulfate (70%) and gel filtration chromatography on Sephacryl S-200. The best inducer and fermentation time for glucanase activities were 5.9 g L-1 and 13 days, respectively. The results revealed three different isoforms (GLUI, GLUII and GLUIII) with purification factors of 4.33,...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Glucanase; Moniliophthora perniciosa; Production; Kinetic characterization; Purification; Heat stability.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652011000200019
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Purification, characterization and structural determination of chitinases produced by Moniliophthora perniciosa Anais da ABC (AABC)
Galante,Rafaela S.; Taranto,Alex G.; Koblitz,Maria G.B.; Góes-Neto,Aristóteles; Pirovani,Carlos P.; Cascardo,Júlio C.M.; Cruz,Sandra H.; Pereira,Gonçalo A.G.; Assis,Sandra A. de.
The enzyme chitinase from Moniliophthora perniciosa the causative agent of the witches' broom disease in Theobroma cacao, was partially purified with ammonium sulfate and filtration by Sephacryl S-200 using sodium phosphate as an extraction buffer. Response surface methodology (RSM) was used to determine the optimum pH and temperature conditions. Four different isoenzymes were obtained: ChitMp I, ChitMp II, ChitMp III and ChitMp IV. ChitMp I had an optimum temperature at 44-73ºC and an optimum pH at 7.0-8.4. ChitMp II had an optimum temperature at 45-73ºC and an optimum pH at 7.0-8.4. ChitMp III had an optimum temperature at 54-67ºC and an optimum pH at 7.3-8.8. ChitMp IV had an optimum temperature at 60ºC and an optimum pH at 7.0. For the computational...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Chitinase; Moniliophthora perniciosa; Kinetic characterization; Purification; Isoenzymes; Heat stability; 3D structure; Comparative modeling.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652012000200016
Registros recuperados: 4
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