島根大学農学部
ISSN:0370-940X
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島根大学農学部研究報告 21
1987-12-21 発行
多重固定化法によって調製した固定化チアミナーゼ I の酵素学的性質
The Enzymological Properties of Immobilized Thiaminase I Prepared by Means of Multi-Immobilization Method
持田 和男
尾添 嘉久
中村 利家
横内 孝行
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内容記述（抄録等）
Thiaminase I (EC 2.5.1.2) was immobilized by the combined use of Sepharose 4B, glutaraldehyde, and K-carrageenan in order to enhance its utility. The native enzyme was inactivated by the addition of organic solvents into an aqueous solution in order to promote the solubility of apolar substrates. However, the multi-immobilized enzymes were not only tolerant to organic solvents but also stable to heat. In addition, the activities of the immobilized enzymes increased during repeated utilizations. Thus, the utility of thiaminase I as a catalyst may be greatly enhanced by the multi-immobilization.
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