Artículos de revistas
Immobilization of a recombinant endo-1,5-arabinanase secreted by Aspergillus nidulans strain A773
Fecha
2012Registro en:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, AMSTERDAM, v. 77, n. 9, supl. 1, Part 1, pp. 39-45, MAY, 2012
1381-1177
10.1016/j.molcatb.2012.01.002
Autor
de Lima Damasio, Andre Ricardo
Pessela, Benevides Costa
Mateo, Cesar
Segato, Fernando
Prade, Rolf Alexander
Guisan, Jose Manuel
Polizeli, Maria de Lourdes Teixeira de Moraes
Institución
Resumen
An endo-1,5-arabinanase (abnA) encoding gene from Aspergillus niveus was identified, cloned and successfully expressed in Aspergillus nidulans strain A773. Based on amino acid sequence comparison, the 34-kDa enzyme could be assigned to CAZy GH family 43. Characterization of purified recombinant endo-1,5-arabinanase (AbnA) revealed that it is active at a wide pH range (pH 4.0-7.0) and an optimum temperature at 70 degrees C. The immobilization of the AbnA was performed via covalent binding onto agarose-modified supports: glyoxyl iminodiacetic acid-Ni2+, glyoxyl amine, glyoxyl (4% and 10%) and cyanogen bromide activated sepharose. The yield of immobilization was similar on glyoxyl amine and glyoxyl (96%), and higher than glyoxyl iminodiacetic acid-Ni2+ (43%) support. The thermal inactivation of these immobilized preparations showed that the stability of the AbnA immobilized on glyoxyl 4 and 10% was improved by 4.0 and 10.3-fold factor at 70 degrees C. The half-life of glyoxyl 4% derivative at 60 degrees C was >48 h (pH 5), 9 h (pH 7) and 88 min (pH 9). The major hydrolysis product of debranched arabinan or arabinopentaose by glyoxyl agarose-immobilized AbnA was arabinobiose. (C) 2012 Elsevier B.V. All rights reserved.