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Effect of pH and temperature on peroxidase and polyphenoloxidase activities of litchi pericarp Scientia Agricola
Mizobutsi,Gisele Polete; Finger,Fernando Luiz; Ribeiro,Rosilene Antônio; Puschmann,Rolf; Neves,Ludmila Lafetá de Melo; Mota,Wagner Ferreira da.
After harvesting litchi, the red color of the fruit pericarp is rapidly lost resulting in discoloration and browning during storage and marketing. The loss of the red color is caused by the degradation or loss of stability of anthocyanins. The action of peroxidase and polyphenoloxidase is usually related to the browning and discoloration of fruits of various species. This study aimed to evaluate the influence of pH and temperature on peroxidase and polyphenoloxidase activities, in a partially purified preparation of pericarp of the litchi cultivar Bengal. Fruits were harvested at the ripe stage and polyphenoloxidase was partially purified by sequential saturation in 80% ammonium sulfate. At concentrations of 40-50% and 60-70% ammonium sulfate the...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Litchi Chinensis Sonn.; Enzyme purification; Skin browning.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-90162010000200013
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Multiple forms of cotyledonary b-galactosidases from Vigna unguiculata quiescent seeds Rev. Bras. Bot.
ENÉAS-FILHO,JOAQUIM; SUDÉRIO,FABRÍCIO BONFIM; GOMES-FILHO,ENÉAS; PRISCO,JOSÉ TARQUÍNIO.
Cotyledonary b-galactosidases were isolated and partially purified from Pitiúba cowpea (Vigna unguiculata (L.) Walp.) quiescent seeds. The purification steps consisted of precipitation of the crude extract with ammonium sulphate in the range of 20-60% saturation, acid precipitation, DEAE-Sephadex ion-exchange chromatography and Lactosyl-Sepharose affinity chromatography. This purification process gave rise to three b-galactosidases-rich fractions: b-gal I, b-gal II and b-gal III, which were purified about 5, 509, and 62 fold, respectively. They reached maximal enzyme activity at different pH ranges: 3.5-4.5 for b-gal I, 3.0-3.5 for b-gal II, and 3.0-4.0 for b-gal III. Their maximal activities were reached when the temperature of the assay medium was 60° C,...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Cotyledons; Cowpea; Enzyme purification; Quiescent seeds.
Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-84042000000100008
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Production and purification of an Endo–1,4-beta-Xylanase from Humicola grisea var. thermoidea by electroelution BJM
Monti,Rubens; Cardello,Leonardo; Custódio,Marcos F.; Goulart,Antonio J.; Sayama,Adriana H.; Contiero,Jonas.
Humicola grisea var. thermoidea produces two forms of extracellular xylanase. The component form 1 was purified using the electroelution method, due to the very small production of this extracellular enzyme. The apparent molecular mass was 61.8 kDa by SDS-PAGE.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Electroelution; Enzyme purification; Extracellular xylanase; Humicola grisea var. thermoidea.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822003000200007
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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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Purification and characterization of xylanases from Trichoderma inhamatum Electron. J. Biotechnol.
Silva,L.A.O; Terrasan,César Rafael Fanchini; Carmona,Eleonora Cano.
Background Two xylanases, Xyl I and Xyl II, were purified from the crude extracellular extract of a Trichoderma inhamatum strain cultivated in liquid medium with oat spelts xylan. Results The molecular masses of the purified enzymes estimated by SDS-PAGE and gel filtration were, respectively, 19 and 14 kDa for Xyl I and 21 and 14.6 kDa for Xyl II. The enzymes are glycoproteins with optimum activity at 50°C in pH 5.0-5.5 for Xyl I and 5.5 for Xyl II. The xylanases were very stable at 40°C and in the pH ranges from 4.5-6.5 for Xyl I and 4.0-8.0 for Xyl II. The ion Hg2+ and the detergent SDS strongly reduced the activity while 1,4-dithiothreitol stimulated both enzymes. The xylanases showed specificity for xylan, Km and Vmax of 14.5, 1.6 mg·mL-1 and 2680.2...
Tipo: Journal article Palavras-chave: Enzyme purification; Physico-chemical properties; Trichoderma inhamatum; Xylanases.
Ano: 2015 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000400009
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Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates Electron. J. Biotechnol.
Fanchini Terrasan,César Rafael; Guisan,José Manuel; Cano Carmona,Eleonora.
Background: Xylanases and β-D-xylosidases are the most important enzymes responsible for the degradation of xylan, the second main constituent of plant cell walls. Results: In this study, the main extracellular xylanase (XYL I) and p-xylosidase (BXYL I) from the fungus Penicillium janczewskii were purified, characterized and applied for the hydrolysis of different substrates. Their molecular weights under denaturing and non-denaturing conditions were, respectively, 30.4 and 23.6 kDa for XYL I, and 100 and 200 kDa for BXYL I, indicating that the latter is homodimeric. XYL I is highly glycosylated (78%) with optimal activity in pH 6.0 at 65°C, while BXYL I presented lower sugar content (10.5%) and optimal activity in pH 5.0 at 75°C. The half-lives...
Tipo: Journal article Palavras-chave: Xylanolytic enzymes; Enzyme characterization; Enzyme purification; Xylan hydrolysis; Xylooligosaccharides hydrolysis.
Ano: 2016 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000500006
Registros recuperados: 6
Primeira ... 1 ... Última
 

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