Purification and characterization of an exo-polygalacturonase from the tomato vascular wilt pathogen Fusarium oxysporum f.sp. lycopersici.

Abstract:

:An exo-polygalacturonase (EC 3.2.1.15) was purified to apparent homogeneity from cultures of Fusarium oxysporum f.sp. lycopersici on synthetic medium supplemented with citrus pectin, using preparative isoelectric focusing. The enzyme, denominated PG2, had an apparent M(r) of 74000 Da upon SDS-PAGE. The pI of the main PG2 isoform was 4.5, and pH and temperature optima were 5.0 and 55 degrees C, respectively. PG2 hydrolyzed polygalacturonic acid in an exo-manner, as demonstrated by anaysis of degradation products. The enzyme was N-glycosylated. The N-terminal amino acid sequence, L-A-F-N-V-P-S-K-P-P, has no identify to other known polygalacturonases.

journal_name

FEMS Microbiol Lett

authors

Di Pietro A,Roncero MI

doi

10.1111/j.1574-6968.1996.tb08592.x

subject

Has Abstract

pub_date

1996-12-01 00:00:00

pages

295-9

issue

2

eissn

0378-1097

issn

1574-6968

pii

S0378109796004272

journal_volume

145

pub_type

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