ABSTRACT

Alpha amylase Inhibitor from Thaumatococcus danielli pulp and seed was Isolated, purified and partially characterized. Gel permeation chromatography of extracts on Sephadex G-200 yielded two peaks (Inhibitor proteins P1 and P2) for the pulp and one peak (inhibitor protein S) for the seed extract. Carbohydrate content of the pulp extract was 4.7Bmg/ml while that of the seed extract was 2.1mg/ml. Purification fraction (fold) obtained alter dialysis of crude extracts were 96.71 and 17.06 for pulp and seed respectively, as against 166.04, 172.82 and 2,09 for Inhibitor proteins P1 and P2 and S.

Optimum pH for all the Inhibitor proteins was 6.5. Incubation of all the inhibitor proteins P1, P2 and S resulted in 9, 4 and 9 percent Inhibition respectively of human salivary amylase.