One endopolygalacturonase from Fusarium moniliforme was purified from the culture broth of a transformed strain of Saccharomyces cerevisiae. Its kinetic parameters and mode of action were studied on galacturonic acid oligomers and homogalacturonan. The dimer was not a substrate for the enzyme. The enzyme was shown to follow Michaelis-Menten behaviour towards the other substrates tested. Affinity and maximum rate of hydrolysis increased with increasing chain length, up to the hexamer or heptamer, for which V-max was in the same range as with homogalacturonan. The enzyme was demonstrated to have a multi-chain attack mode of action and its active site included five subsites ranging from -3 to +2. The final products of hydrolysis of homogalacturonan were the monomer and the dimer of galacturonic acid. (C) 2001 Elsevier Science B.V. All rights reserved.
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1016/S0304-4165(01)00141-6|
|Codice identificativo ISI:||WOS:000169535500011|
|Codice identificativo Scopus:||2-s2.0-0035877157|
|Titolo:||Study of the mode of action of endopolygalacturonase from Fusarium moniliforme|
|Appare nelle tipologie:||1.1 Articolo in rivista|