BioChem - DOS

An acidic thermostable recombinant Aspergillus nidulans endoglucanase is active towards distinct agriculture residues

Enzyme research

Tavares, Eveline Queiroz de Pinho; Rubini, Marciano Regis; Mello-de-Sousa, Thiago Machado; Duarte, Gilvan Caetano; de Faria, Fabrí cia Paula; Ferreira Filho, Edivaldo Ximenes; Kyaw, Cynthia Maria; Silva-Pereira, Ildinete; Poç as-Fonseca, Marcio Jose

<P><I>Aspergillus nidulans</I> is poorly exploited as a source of enzymes for lignocellulosic residues degradation for biotechnological purposes. This work describes the <I>A. nidulans</I> Endoglucanase A heterologous expression in <I>Pichia pastoris</I>, 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 <I>K</I><SUB><I>m</I></SUB> = 27.5 ± 4.33 mg/mL, <I>V</I><SUB>max</SUB> = 1.185 ± 0.11 mmol/min, and 55.8 IU (international units)/mg specific activity. Recombinant <I>P. pastoris</I> 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.</P>

2013

Hindawi Publishing Corporation

cc-by

2090-0406

2090-0414

2013

pp.287343

10.1155/2013/287343

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART74497473

https://downloads.hindawi.com/archive/2013/287343.pdf