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

• Published in: Enzyme and microbial technology Vol. 12; no. 2; pp. 120 - 123
• Main Authors: Yazdi, M.T., Radford, A., Keen, J.N., Woodward, J.R.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 01.02.1990; Elsevier Science
• Subjects: Amino Acid Sequence; beta -glucosidase; Biological and medical sciences; Biotechnology; cellulase; Cellulase - biosynthesis; Cellulase - isolation & purification; cellulolytic enzymes; cellulose 1,4- beta -cellobiosidase; Chromatography, Gel - methods; Chromatography, Ion Exchange - methods; Endoglucanase; Enzyme engineering; exoglucanase; Fundamental and applied biological sciences. Psychology; Improved methods for extraction and purification of enzymes; Methods. Procedures. Technologies; Molecular Sequence Data; Molecular Weight; Neurospora - enzymology; Neurospora crassa - enzymology; purification; β-glucosidase; Endoglucanase; exoglucanase; β-glucosidase; purification; Purification; β-D-Glucosidase; Molecular weight determination; Enzyme; Ion exchange chromatography; Fungi; Characterization; Cellulase; Exo-cellobiohydrolase; Gel filtration; Ascomycetes; Neurospora crassa; Thallophyta; Chromatofocusing
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/0141-0229(90)90084-4

In studies on cellulase production by the cell-1 mutant of Neurospora crassa, eight enzymes (three exoglucanases, four endoglucanases, and one β-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%.