Open AccessPurification and characterization of an acidic endo‐β‐1,4‐xylanase from the tomato vascular pathogen Fusarium oxysporum f. sp. lycopersici
Author(s) -
Ruiz M.Carmen,
Pietro Antonio,
Roncero M.Isabel G
Publication year - 1997
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.1574-6968.1997.tb10270.x
Subject(s) - fusarium oxysporum , xylanase , fusarium oxysporum f.sp. lycopersici , isoelectric point , enzyme , isoelectric focusing , biochemistry , xylan , fungi imperfecti , fusarium , biology , fungus , chemistry , microbiology and biotechnology , botany , fusarium wilt
Fusarium oxysporum f. sp. lycopersici produced at least one acidic and one basic xylanase when grown on synthetic minimal medium supplemented with tomato vascular tissue as the sole carbon source. An acidic endo‐β‐1,4‐xylanase (EC 3.2.1.8) was purified to apparent homogeneity from cultures of the fungus grown on xylan, using preparative isoelectric focusing. The enzyme denominated XYL1 had a M r of 40 kDa upon SDS PAGE and a pI of 3.7. The pH and temperature optima were 4.5 and 40°C, respectively. The enzyme was N ‐glycosylated. The N‐terminal amino acid sequence (Glu, Val, Ala, Pro, Val, Phe, Asn, Ile, Asp, Asp, Lys) showed no homology with other known xylanases.