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Rhizopus delemar glucoamylase GIII (Mw 78, 000) was converted into a new form, G' (Mw 72, 000), through the limited action of chymotrypsin. With the modification, its ability of adsorption on starch granules and high affinity for water-soluble polysaccharides decreased due to the removal of the postulated specific affinity site for polysaccharides, the "starch-binding site." The peptide (s), released on the modification, reduced the adsorption on raw-starch granules and the hydrolysis of glycogen with the enzymes. These results suggest that the peptide (s) is the starch-binding site (s) itself or a part of it.

Removal of the starch-binding site of Rhizopus delemar glucoamylase by limited proteolysis with chymotrypsin.