MULTIPLE FORMS OF PECTIC LYASES AND POLYGALACTURONASE FROM FUSARIUM-OXYSPORUM F-SP RADICIS LYCOPERSICI - REGULATION OF THEIR SYNTHESIS BY GALACTURONIC ACID
Ma. Guevara et al., MULTIPLE FORMS OF PECTIC LYASES AND POLYGALACTURONASE FROM FUSARIUM-OXYSPORUM F-SP RADICIS LYCOPERSICI - REGULATION OF THEIR SYNTHESIS BY GALACTURONIC ACID, Canadian journal of microbiology, 43(3), 1997, pp. 245-253
The r2 isolate of Fusarium oxysporum f.sp. radicis-lycopersici produce
d several pectic enzymes that differ in substrate preference, reaction
mechanism, and action pattern. We detected three forms that have lyas
e activity, four forms with polygalacturonase activity and one form wi
th pectinesterase activity. Lyases had an absolute requirement for cal
cium and pIs of 9.20, 9.00, and 8.65. The two more alkaline forms had
a weak preference for pectin, whereas the other was mon active on poly
galacturonate. Polygalacturonases had pIs of 9.30, 7.35, 6.85, and 6.5
5 and were inhibited by calcium ions. Lyases and polygalacturonases we
re induced by galacturonic acid and were subject to catabolite repress
ion. Induced synthesis occurred at pHs 5.5 and 8.0 and no increase in
lyase activities were promoted by alkalinization of cultures. Pectin l
yase had an endo mode of action, whereas pectate lyase and polygalactu
ronase behaved more as exoenzymes. These results are discussed in rela
tion to the appearance of the different pectic enzymes when the fungus
is confronted with a pectic polymer.