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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Co-immobilization of fungal endo-xylanase and alpha-L-arabinofuranosidase in glyoxyl agarose for improved hydrolysis of arabinoxylan

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Author(s):
de Lima Damasio, Andre Ricardo [1] ; Pessela, Benevides C. [2] ; da Silva, Tony Marcio [3] ; Souza Guimaraes, Luis Henrique [3] ; Jorge, Joao Atilio [3] ; Manuel Guisan, Jose [4] ; Polizeli, Maria de Lourdes T. M. [3]
Total Authors: 7
Affiliation:
[1] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Bioquim & Imunol, BR-14040901 Ribeirao Preto, SP - Brazil
[2] CIAL CSIC, Inst Ciencias Alimentac, Dept Biotecnol & Microbiol Alimentos, Madrid 28049 - Spain
[3] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Biol, BR-14040901 Ribeirao Preto, SP - Brazil
[4] Inst Catalisis & Petroleoquim CSIC, Dept Biocatalisis, Madrid 28049 - Spain
Total Affiliations: 4
Document type: Journal article
Source: JOURNAL OF BIOCHEMISTRY; v. 154, n. 3, p. 275-280, SEP 2013.
Web of Science Citations: 6
Abstract

Plant cell-wall arabinoxylans have a complex structure that requires the action of a pool of debranching (arabinofuranosidases) and depolymerizing enzymes (endo-xylanase). Two Aspergillus nidulans strains over-secreting endo-xylanase and arabinofuranosidase were inoculated in defined 2% maltose-minimum medium resulting in the simultaneously production of these enzymes. To study the synergistic hydrolysis was used arabinoxylan with 41% of arabinose and 59% of xylose residues. Thus, it was adopted different approaches to arabinoxylan hydrolysis using immobilized arabinofuranosidase and endo-xylanase: (i) endo-xylanase immobilized on glyoxyl agarose; (ii) arabinofuranosidase immobilized on glyoxyl agarose; (T-1) hydrolysis of arabinoxylan with arabinofuranosidase immobilized on glyoxyl agarose for debranching, followed by a second hydrolysis with endo-xylanase immobilized on glyoxyl agarose; (T-2) hydrolysis using (i) and (ii) simultaneously; and (T-3) hydrolysis of arabinoxylan with endo-xylanase and arabinofuranosidase co-immobilized on glyoxyl agarose. It was concluded that arabinoxylan hydrolysis using two derivatives simultaneously (T-2) showed greater hydrolytic efficiency and consequently a higher products yield. However, the hydrolysis with multi-enzymatic derivative (T-3) results in direct release of xylose and arabinose from a complex substrate as arabinoxylan, which is a great advantage as biotechnological application of this derivative, especially regarding the application of biofuels, since these monosaccharides are readily assimilable for fermentation and ethanol production. (AU)