Cellulase production by Neurospora crassa: purification and characterization of cellulolytic enzymes.
In studies on cellulase production by the cell-1 mutant of Neurospora crassa, eight enzymes (three exoglucanases, four endoglucanases, and one beta-glucosidase) were identified and characterized by gel filtration, ion exchange chromatography, and chromatofocusing. After purification, each of the proteins ran as a single band in polyacrylamide gel electrophoresis, using both native and denaturing gels. The molecular weights of the proteins were found to be between 70,000 and 22,000 daltons, and all were glycosylated, with carbohydrate contents ranging between 5.6% and 36%.
Yazdi
M T
MT
Biotechnology Unit, University of Leeds, UK.
Radford
A
A
Keen
J N
JN
Woodward
J R
JR
D000595:Amino Acid Sequence; D002480:Cellulase / Q000096:biosynthesis / Q000302:isolation & purification*; D002850:Chromatography, Gel / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology*
D002480:Cellulase