期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 77, 期 -, 页码 39-45出版社
ELSEVIER
DOI: 10.1016/j.molcatb.2012.01.002
关键词
Aspergillus niveus; Aspergillus nidulans; Recombinant endo-1,5-arabinanase; Over-expression; Purification; Immobilization
资金
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
- Conselho de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Banco SANTANDER S.A.
- Department of Energy [06103-OKL, ZDJ-7-77608-01]
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.
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