초록

용어보기논문에서 용어와 풀이말을 자동 추출한 결과로, 시범 서비스 중입니다. AI-Helper

Abstract ▼ AI-Helper

Glucose oxidase (GOD) was immobilized by polyacrylamide entrapment to use respeatedly for the determination of glucose in blood and hydrolyzates of polysaccharides. The retained activity of immobilized GOD was about 80 % when 1~2 unit of the native GOD was applied for immobilization, but the GOD act...

Glucose oxidase (GOD) was immobilized by polyacrylamide entrapment to use respeatedly for the determination of glucose in blood and hydrolyzates of polysaccharides. The retained activity of immobilized GOD was about 80 % when 1~2 unit of the native GOD was applied for immobilization, but the GOD activity was not retained in proportion to increment of GOD unit. The immobilized GOD had 85.5% of the ratained activity for 0.3 mm of bead diameter. The enzyme activity, however, decreased as size of of bead increased. In pH stability of the enzyme, the residual activity of the native GOD was 60% when the enzyme was pretreated at pH 5.5 for 10 hr, while the residual activity of immobilized one was about 80% when at pH 5.5~6.5. The GOD had higher thermal stability when the native enzyme was preincubated at $35{\sim}50{\circ}C$ for 10 hr and immobilized one at $35{\sim}60{\circ}C$. There was no significant decrease of the immobilized enzyme activity by using repeatedly in batch reactor one time per day for 30 times. The retained activity of immobilized GOD decrease remarkably when the product was stored at room temperature for 4 months in dry state. Lyophilized enzyme and the enzyme in phosphate buffer solution at $-5{\cirs}C$ showed a tendency to decrease depending on the storage period. The linear curve was obtained by determination of various concentrations of D-glucose by the immobilized GOD.