Abstract
The mode of action of the endopolygalacturonase from Fusarium moniliforme was studied towards a series of pectins with different amounts and distribution patterns of substituents. In homogalacturonan, the enzyme hydrolysed the linkages between two galacturonic acid residues according to a multi-chain attack mechanism, and the final products were monomer and dimer. The enzyme was able to degrade methylated pectins with a degree of methylation up to 70 and acetylated homogalacturonans with a degree of acetylation up to 38 to a lower extend but not xylogalacturonans.
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