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An Acidic Thermostable Recombinant Aspergillus nidulans Endoglucanase Is Active towards Distinct Agriculture Residues

2013; Hindawi Publishing Corporation; Volume: 2013; Linguagem: Inglês

10.1155/2013/287343

2090-0406

Eveline Queiroz de Pinho Tavares, Marciano Régis Rubini, Thiago Machado Mello-de-Sousa, Gilvan Caetano Duarte, Fabrícia Paula de Faria, Edivaldo Ximenes Ferreira Filho, Cynthia Maria Kyaw, Ildinete Silva-Pereira, Márcio José Poças-Fonseca,

Enzyme Catalysis and Immobilization

Aspergillus nidulans is poorly exploited as a source of enzymes for lignocellulosic residues degradation for biotechnological purposes. This work describes the A. nidulans Endoglucanase A heterologous expression in Pichia pastoris , the purification and biochemical characterization of the recombinant enzyme. Active recombinant endoglucanase A (rEG A) was efficiently secreted as a 35 kDa protein which was purified through a two-step chromatography procedure. The highest enzyme activity was detected at 50 ° C/pH 4. rEG A retained 100% of activity when incubated at 45 and 55 ° C for 72 h. Purified rEG A kinetic parameters towards CMC were determined as K m = 27.5 ± 4.33 mg/mL, V max = 1.185 ± 0.11 mmol/min, and 55.8 IU (international units)/mg specific activity. Recombinant P. pastoris supernatant presented hydrolytic activity towards lignocellulosic residues such as banana stalk, sugarcane bagasse, soybean residues, and corn straw. These data indicate that rEG A is suitable for plant biomass conversion into products of commercial importance, such as second-generation fuel ethanol.