Separation and partial purification of beta-glucosidase and two endoglucanases in Aspergillus niveus.
The thermotolerant Aspergillus niveus strain RMF 7883 was grown in Czapek medium, with filter paper cellulose. The proportion of mycelial-bound to extracellular enzymes was studied. Most of the beta-glucosidase (80.9%) and endoglucanases (78.3%) activities were extracellular. The extracellular endoglucanases and beta-glucosidase were separated and partially purified by Sephadex G-100 gel filtration, followed by ion exchange chromatography on CM-trisacryl M. Two extracellular endoglucanases, EG I and EG II (130 kDa and 35 kDa, respectively), and beta-glucosidase (194 kDa) were isolated from culture filtrate.
Taj-Aldeen
S J
SJ
Department of Biology, College of Science, University of Babylon, Hilla, Iraq.
Alkenany
K I
KI
D001233:Aspergillus nidulans / Q000201:enzymology*; D002480:Cellulase / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005110:Extracellular Space / Q000201:enzymology; D005656:Fungal Proteins / Q000302:isolation & purification*; D008970:Molecular Weight; D001617:beta-Glucosidase / Q000302:isolation & purification*
D005656:Fungal Proteins; D001617:beta-Glucosidase; D002480:Cellulase