Open AccessPurification and characterization of an extracellular endo‐1,4‐β‐xylanase from Fusarium oxysporum f. sp. melonis
Author(s) -
Alconada T.M.,
Martínez M.J.
Publication year - 1994
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.1574-6968.1994.tb06845.x
Subject(s) - xylanase , fusarium oxysporum , size exclusion chromatography , xylose , molecular mass , xylan , chemistry , chromatography , enzyme , extracellular , gel electrophoresis , biochemistry , polyacrylamide gel electrophoresis , biology , botany , fermentation
Fusarium oxysporum f. sp. melonis produces extracellular endo‐1,4‐β‐xylanase and β‐xylosidase when grown in shaken culture at 26°C in a mineral salts medium containing oat spelt xylan and glucose as carbon sources. Endo‐1,4‐β‐xylanase was purified 251 times from 5‐day‐old culture filtrates, by Sephacryl S‐200, ion exchange and gel filtration HPLC. The purified sample yielded a single band in SDS polyacrylamide gels with a molecular mass of 80 kDa on electrophoretic mobility and 83 kDa by gel filtration behavior. High activity of the endo‐1,4‐β‐xylanase against xylan was observed between 5 and 8 pH, and between 40 and 60°C, the optimum pH and temperature being 5.0 and 50°C, respectively. Kinetic properties of the enzyme are similar to those of other fungal xylanases, showing high affinity towards oat spelt xylan with a K m of 1 mM expressed as xylose equivalent.