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Mycelial glucoamylases produced by the thermophilic fungus Scytalidium thermophilum strains 15.1 and 15.8: purification and biochemical characterization BJM
Ferreira-Nozawa,M.S.; Rezende,J.L.; Guimarães,L.H.S.; Terenzi,H.F.; Jorge,J.A.; Polizeli,M.L.T.M..
Two strains (15.1 and 15.8) of the thermophilic fungus Scytalidium thermophilum produced high levels of intracellular glucoamylases, with potential for industrial applications. The isoform I of the glucoamylase produced by 15.1 strain was sequentially submitted to DEAE-Cellulose and CM-Cellulose chromatography, and purified 141-fold, with 5.45% recovery. The glucoamylase of strain 15.8 was purified 71-fold by CM-Cellulose and Concanavalin A-Sepharose chromatography, with 7.38% recovery. Temperature and pH optima were in the range of 50-60ºC and 5.0-6.0, respectively, using starch and maltose as substrates. The glucoamylase of S. thermophilum 15.8 was more stable (t50 > 60 min) than that of S. thermophilum 15.1 (t50= 11-15 min), at 60ºC. The glucoamylase...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Glucoamylase; Amylase; Scytalidium thermophilum; Thermostable enzyme; Starch hydrolysis.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000200027
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