Cellulase production by Neurospora crassa: purification and characterization of cellulolytic enzymes

Enzyme Microb Technol. 1990 Feb;12(2):120-3. doi: 10.1016/0141-0229(90)90084-4.

Abstract

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%.

MeSH terms

  • Amino Acid Sequence
  • Cellulase / biosynthesis
  • Cellulase / isolation & purification*
  • Chromatography, Gel / methods
  • Chromatography, Ion Exchange / methods
  • Molecular Sequence Data
  • Molecular Weight
  • Neurospora / enzymology*
  • Neurospora crassa / enzymology*

Substances

  • Cellulase