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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.

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