吸着剤表面における酵素の動態

概要

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Glucoamylase was adsorbed on an adsorbent in order to obtain insoluble enzyme. Through the reaction catalyzed by the enzyme-adsorbent compled, a part of the adsorbed emzyme eluted from the adsorbent, but the rest still remained on the surface of the adsorbent. The activity of both parts of enzyme decreased in comparison with that of native one. Moreover, about the kinetic constants, an increse in the Michaelis constant and a decrease in the maximum velocity were observed. Althogh it is reasonable that the activity of the enzyme absorbed on the surface of the adsorbent should decrease, varying its dimensional structure, it was found that the eluted enzyme was also slightly denaturated. The behavions of both adsorbed and native enzymes were almost the same in case they were inhibited by mercuric acetate. It was assumed that the mechanism of inhibition of the adsorbed enzyme was similar to that of the native one. With a decrease in molecular weight of the substrate, the Michaelis constant increased, but the maximum velocity remained constant. The difference in kinetic constants between the adsorbed enzyme and the native one became smaller with a decrease in molecular weight of the substrate. It was assumed that the influence of the steric hindrance by the adsorbent on the smaller substrate was insignificant.
社団法人日本生物工学会の論文
1970-08-25