Xylanolytic complex from Aspergillus giganteus: production and characterization.
An Aspergillus giganteus strain was isolated as an excellent producer of xylanase associated with low levels of cellulase. Optimal xylanase production was obtained in liquid Vogel medium containing xylan as carbon source, pH 6.5 to 7.0, at 25 degrees C and under shaking at 120 rpm during 84 h. Among the several carbon sources tested, higher xylanase production was verified in xylan, xylose, sugar-cane bagasse, wheat bran and corn cob cultures, respectively. Optimal conditions for activity determination were 50 degrees C and pH 6.0. The xylanolytic complex of A. giganteus showed low thermal stability with T(50) of 2 h, 13 min and 1 min when it was incubated at 40, 50 and 60 degrees C, respectively, and high stability from pH 4.5 to 10.5, with the best interval between 7.0 to 7.5. This broad range of stability in alkali pH indicates a potential applicability in some industrial processes, which require such condition. Xylanolytic activity of A. giganteus was totally inhibited by Hg(+2), Cu(+2) and SDS at 10 mM. The analysis of the products from the oat spelts xylan hydrolysis through thin-layer chromatography indicated endoxylanase activity, lack of debranching enzymes and beta-xylosidase activity in assay conditions.
Coelho
Glauciane Danusa
GD
Departamento de Bioquímica e Microbiologia, Instituto de Biociências, UNESP, 13506-900, Rio Claro, SP, Brasil.
Carmona
Eleonora Cano
EC
D001230:Aspergillus / Q000201:enzymology*; D004795:Enzyme Stability; D005656:Fungal Proteins / Q000096:biosynthesis*; D006863:Hydrogen-Ion Concentration; D013696:Temperature; D043325:Xylan Endo-1,3-beta-Xylosidase; D014995:Xylosidases / Q000096:biosynthesis* / Q000737:chemistry
D005656:Fungal Proteins; D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase