CAJ | 학술논문

为了探索绿豆酯酶的固定化方法,对阴离子交换树脂D261、D280、D301、D380酸碱处理后,通过离子交换吸附法来固定绿豆酯酶,筛选出固定效果较好的阴离子交换树脂D380,并进行固定化条件的优化研究.考查了固定化温度、固定化时间和粗酶液稀释倍数对固定化绿豆酯酶活力的影响,通过响应面法优化绿豆酯酶的固定条件.结果表明较佳的固定化条件为:粗酶液稀释25倍,固定化温度为30℃,固定化时间为3.0h.实际测得固定化绿豆酯酶活力为0.825 1U/g,与理论预测值相对误差为-1.7%,二者基本吻合.
위료탐색록두지매적고정화방법,대음리자교환수지D261、D280、D301、D380산감처리후,통과리자교환흡부법래고정록두지매,사선출고정효과교호적음리자교환수지D380,병진행고정화조건적우화연구.고사료고정화온도、고정화시간화조매액희석배수대고정화록두지매활력적영향,통과향응면법우화록두지매적고정조건.결과표명교가적고정화조건위:조매액희석25배,고정화온도위30℃,고정화시간위3.0h.실제측득고정화록두지매활력위0.825 1U/g,여이론예측치상대오차위-1.7%,이자기본문합.
To explore imobilization method of mung bean esterase, four types of anion exchange resins D261, D280, D301and D380 were treated using a given content acid and alkali solutions, and applied to imobilze mung bean esterase. Anion exchange resin D380 was better immobilization effect and its immobilization conditions were optimized. Based on single factor and response surface method experiments , immobilization conditions of mung bean esterase were investigated. Results showed that optimun immobilization conditions were a diluted 25 times of original enzyme solution, an immobilization temperature of 30℃, and an immobilization time of 3 hours. Under these conditions, imobilized mung bean esterase activity was 0.825 1 U/g, relative error between determined and predicted value was-1.7 %, and tested and predicted value was similar basically.