ブリ幽門垂Carboxylesteraseの性状について〔ハマチ脂質分解酵素に関する研究-2-〕

概要

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The purification of carboxylesterase (EC 3.1.1.1) in the pyloric caeca extract of young yellowtail, Seriola quinqueradiata, was accomplished by chromatographies on columns of DEAE-cellulose and Sephadex G-100 and G-200. The final preparations (PS-1-1 and PS-2) were homogeneous in poly-acrylamide gel disc electrophoresis at pH9.4. The molecular weight and the isoelectric point of PS-1-1 were estimated to be over 450, 000 and pH4.7, respectively. The optimum pH of PS-1-1 was 7.0 and the enzyme showed the highest enzyme activity at 40°C. This esterase was stable between pH5.5 to 7.5, and below 30°C. Km of PS-1-1 was estimated to be 1.0×10-4M. PS-1-1 was inhibited by some metal ions and reagents such as Hg+2, Zn+2, Mg+2, Ni+2, CH2ICOOH and p-chloromercuribenzoate. On the other hand, PS-2 had the molecular weight of approximately 52, 000, the isoelectric point at pH5.6. The optimum pH of PS-2 was 8.0 and the enzyme showed the highest enzyme activity at 40°C. The PS-2 was stable between the pH range of 7.5 to 8.5, and below 30°C. Km of PS-2 was 1.6×10-4M, and PS-2 was inhibited by Hg+2.
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