Open AccessPurification and characterization of a neutral endoxylanase from Aspergillus nidulans
Author(s) -
FernándezEspinar María Teresa,
Piñaga Francisco,
Sanz Pascual,
Ramón Daniel,
Vallés Salvador
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06518.x
Subject(s) - aspergillus nidulans , isoelectric point , biochemistry , enzyme , molecular mass , xylan , isoelectric focusing , chemistry , xylanase , chromatography , biology , mutant , gene
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°C and had a K m of 4.2 mg oat spelt xylan per ml and a V max of 710 μmol min −1 (mg protein) −1 .