title: Purification and some properties of a xylanase from Aspergillus sydowii MG49.
abstract: Aspergillus sydowii MG49 produces a 30-kDa exosplitting xylobiohydrolase during growth on xylan. A specific chemical modification and substrate protection analysis of purified xylanase provided evidence that tryptophan and carboxy and amino groups are present at the catalytic site of this enzyme. Thermal inactivation of the xylanase occurs because of irreversible polymolecular aggregation, which is slower in the presence of glycerol.
authors: Department of Microbiology, Bose Institute, Calcutta, India.
authors: M
authors: M
authors: Ghosh
authors: G
authors: G
authors: Nanda
mesh_terms: D001230:Aspergillus / Q000201:enzymology*; D004187:Disaccharides / Q000378:metabolism; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D043325:Xylan Endo-1,3-beta-Xylosidase; D014990:Xylans / Q000378:metabolism; D014995:Xylosidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D004187:Disaccharides; D014990:Xylans; D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase; C004173:xylobiose