[Purification of exo-1,4-beta-xylosidase from Aspergillus niger 15].
From the preparation of xylanase of the fungus Aspergillus niger 15 exo-1,4-beta-xylosidase was isolated by means of ethanol fractionation and chromatography on columns of Sephadex G-50, cellulose DE-52, Sephadex SP C-50, Sephadex G-200. The isolated enzyme (with the purification degree as calculated per protein 199, and yield with respect to activity 42.5%) was homogeneous during gel filtration, polyacrylamide gel electrophoresis in the presence and absence of Na dodecyl sulfate, ultracentrifugation and isoelectric focusing. Exo-1,4-beta-xylosidase had a molecular mass of 253,000 as shown by gel filtration and 122,000 as shown by Na dodecyl sulfate polyacrylamide gel electrophoresis; its sedimentation coefficient was 10.6 S and isoelectric point was pI 4.9. The specific activity of the homogeneous enzyme was 35.2 u./mg protein with respect to p-nitrophenyl-beta-D-xylopyranoside and 30.2 u./mg protein with respect to xylobiose.
D001234:Aspergillus niger / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005285:Fermentation; D006026:Glycoside Hydrolases / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008970:Molecular Weight; D014462:Ultrafiltration; D014995:Xylosidases / Q000302:isolation & purification*
D006026:Glycoside Hydrolases; D014995:Xylosidases; C026579:exo-1,4-beta-D-xylosidase
Ochistka ékzo-1,4-beta-ksilozidazy Aspergillus niger 15.