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Purification and characterization of a thermostable a-amylase produced by the fungus Paecilomyces variotii

Michele Michelin, Tony M. Silva, Vivian M. Benassi, Simone C. Peixoto-Nogueira, Luiz Alberto B. Moraes, Juliana M. Leão, João A. Jorge, Héctor F. Terenzi, Maria de Lourdes T. M. Polizeli


Carbohydrate Research 345 (2010) 2348–2353


An a-amylase produced by Paecilomyces variotii was purified by DEAE-cellulose ion exchange chromatography, followed by Sephadex G-100 gel filtration and electroelution. The a-amylase showed a molecular mass of 75 kDa (SDS–PAGE) and pI value of 4.5. Temperature and pH optima were 60ºC and 4.0, respectively. The enzyme was stable for 1 h at 55ºC, showing a t50 of 53 min at 60 ºC. Starch protected the enzyme against thermal inactivation. The a-amylase was more stable in alkaline pH. It was activated mainly