不溶化細菌液化型α-アミラーゼの調製とその性質

概要

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Bacterial α-amylase of liquefying type was immobilized by covalent bonding on Sepharose 4B, which was activated with cyanogen bromide. The specific activity of the immobilized α-amylase was 2.2% of that of the native α-amylase when assayed by the Blue value method. The optimum pH and the optimum temperature of the immobilazed α-amylase were same as those of the native enzyme, but the pH and thermal stability of the immobilized enzyme were higher than those of the native enzyme.The degradation pattern of soluble starch with the immobilized α-amylase differed from that with the native enzyme. That is, the ratio of saccharifying activity to liquefying activity of the immobilized α-amylase was changed to that of the native bacterial saccharifying α-amylase type. However, the final extent of hydrolysis and end products of soluble starch with the immobilized α-amylase were almost the same as those of the native liquefying α-amylase. The most likely explanation of this result may be a steric hindrance.
社団法人日本生物工学会の論文
1977-03-25