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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
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