清酒醸造における酵素バランスについて : (第2報)とくに醪中 amylase の動力学的検討

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In sake-brewing, steamed rice in the mash is digested by hydrolytic enzymes of Aspergillus oryzae. In constructing kinetic models for the reaction rates, it is assumed that the amount of enzyme-substrate complex, which determines the rate, is proportional to the product of the n-th power (n=1 in the case of glucamylas) of free enzyme concentration in liquid phase and the area of free (unoccupied) substrate surface. Rate equations have been deduced from the above assumption. The results with the system of enzyme solution-steamed rice showed that the above rate equations were satisfactory. For instance, the following equation was shown to be in accord with the observed initial reaction velocity (υ_0,mg dissolved total sugar as glucose/ml. hr) of α-amylase at 11℃ and pH 4.8 : υ_0=([E_0]^1/3・S_0)/(132+26[E_0]^1/3)V where [E_0], S_0 and V are the initial enzyme concentration (units per ml of liquid phase), the initial quantity of substrate (steamed rice, mg as glucose) and the volume of liquid phase (ml), respectively. The equation is valid in the case where there is no "ineffective" adsorption (adsorption which does not lead to the formation of effective enzyme-substrate complex) of α-amylase on the substrate. In the case of glucamylase, the following equations for V_0 (mg glucose/ml. hr) were maintained at 11℃ and pH 4.8 : υ_0=([E_0]・S_0)/(1900V+200V[E_0]+6S_0) for Asp. oryzae-amylase; υ_0=([E_0]・S_0)/(3800V+200V[E_0]+6S_0) for Asp. niger-amylase.The difference in the above two expressions is regarded to be due to the difference in the K-values (distribution coefficient of glucamylase between solid and liquid phases).
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清酒醸造における酵素バランスについて : (第2報)とくに醪中 amylase の動力学的検討

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