When the glucoamylase protein immobilized to Amberlite IRA-904 was est
imated by direct (Kjeldhal), indirect (measuring the protein left in t
he supernatant) and elution methods, direct and indirect methods gave
almost same results while the elution method gave a protein concentrat
ion of only 68.9% of that obtained with the Kjeldhal method. When the
activity of the soluble and immobilized glucoamylase were compared wit
h different substrates, the activity yield increased with decreasing m
olecular size of the substrate. However when the immobilized glucoamyl
ase containing Amberlite IRA-904 was pound, it Showed increase in acti
vity with increasing molecular weight of the substrates.