Purification and characterization of a neutral endoxylanase from Aspergillus nidulans

A neutral endoxylanase from a culture filtrate of Aspergillus nidulans grown on oat spelt xylan was purified to apparent homogeneity. The purified enzyme showed a single band on SDS-PAGE with a molecular mass of 22,000 and had an isoelectric point of 6.4. The enzyme was a non-debranching endoxylanas...

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Bibliographic Details
Published in:FEMS microbiology letters 1993, Vol.113 (2), p.223-228
Main Authors: Fernandez-Espinar, M.T, Pinaga, F, Sanz, P, Ramon, D, Valles, S
Format: Article
Language:English
Subjects:
Aspergillus nidulans
Aspergillus nidulellus
Biological and medical sciences
Biotechnology
culture filtrates
Fundamental and applied biological sciences. Psychology
Growth, nutrition, metabolism, transports, enzymes. Molecular biology
Microbiology
Mycology
O-glycoside hydrolases
physicochemical properties
Purification
xylan
Xylanase
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Summary:A neutral endoxylanase from a culture filtrate of Aspergillus nidulans grown on oat spelt xylan was purified to apparent homogeneity. The purified enzyme showed a single band on SDS-PAGE with a molecular mass of 22,000 and had an isoelectric point of 6.4. The enzyme was a non-debranching endoxylanase highly specific for xylans and completely free from cellulolytic activity. The xylanase showed an optimum activity at pH 5.5 and 62 degrees C and had a Km of 4.2 mg oat spelt xylan per ml and a Vmax of 710 micromolar min-1 (mg protein)-1.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1993.tb06518.x