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| 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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| 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 |
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| Neves,Valdir Augusto; Lourenço,E. J.. |
| Peroxidase from peach fruit was purified 28.9-fold by DEAE-cellulose, Sephadex G-100 and hydroxylapatite chromatography. The purified enzyme showed only one peak of activity with an optimum pH of 5.0 and temperature of 40ºC. The calculated activation energy (Ea) for the reaction was 7.97 kcal/mol. The enzyme was heat-labile in the temperature range of 60 to 80ºC with a fast inactivation at 80ºC. PAGE of the inactivation course at 70ºC showed only one band of activity. Different sugars increased the heat stability of the activity in the following order: sucrose>lactose>glucose>fructose. Measurement of residual activity showed a stabilizing effect of sucrose at various temperature/sugar concentrations (10 to 40%, w/w) with the Ea for inactivation... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Peach peroxidase; Purification; Heat stability; Regeneration. |
| Ano: 1998 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89131998000200002 |
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| Neves,Valdir Augusto. |
| Soluble, ionically bound peroxidase (POD) and polyphenoloxidase (PPO) were extracted from the pulp of peach fruit during ripening at 20°C. Ionically bound form was purified 6.1-fold by DEAE-cellulose and Sephadex G-100 chromatography. The purified enzyme showed only one peak of activity on Sephadex G-100 and PAGE revealed that the enzyme was purified by the procedures adopted. The purified enzyme showed a molecular weight of 29000 Da, maximum activity at pH 5.0 and at 40ºC. The calculated apparent activation energy (Ea) for the reaction was10.04 kcal/mol. The enzyme was heat-labile in the temperature range of 60 to 75ºC with a fast inactivation at 75ºC. Measurement of residual activity showed a stabilizing effect of sucrose at various temperature/sugar... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Peach peroxidases; Ripening; Purification; Kinetics; Heat stability. |
| Ano: 2002 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132002000100002 |
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