酵素剤による蒸米の糖化溶解機構

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The enzymic digestion of parboiled rice (α-rice) was analyzed from the viewpoint of the reaciton kinetics.1. α-Amylase activity in an aqueous solution of Takadiastase-A decreased during the digestion of rice because of the adsorption of the enzyme on α-rice.2. Glucamylse added to the Takadiastase-A solution lowerd the rate of α-amylase adsorption. An addition of NaCl (0.5%) prevented the adsorption of α-amylase almost completely. In both cases the digestion of rice proceeded well, especially in the latter case, These results suggest that only α-amylse in the solution contributes to the reaciton .Conversely, the adsorbed enzyme is inactive.3. Assuming an enzyme-substrate complex (which should be different from the adsorbed α-amylse mentioned above) is formed on the active surface of the rice grain in equillibrium with the free α-amylase in the solution, a reaction model may be presented as : -(ds)/(dt) =kE^αs^β, where s is the content of residual substrate (fraction), E is the α-amylase activity in the solution, t is time, and k, α, β are constants.4. The changes of the α-amylase actibity in the reaction solution (cf. Figs. 1 to 4) were simulated by the function of time. Substituing these functions in to the kinetic model, the respective dissolution curves could be calculated numerically by using a digital computer.5. The results of the calculation could explain the experimental data fairly successfully. The calues of the constants were determined as ; k=0.02(U/ml)^<-α>hr^<-1>α=0.3(dimensionless)β=1(dimensionless).
社団法人日本生物工学会の論文

酵素剤による蒸米の糖化溶解機構

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