摘要
本文研究了用吸附交联技术共固定化蔗糖酶和葡萄糖氧化酶(GOD)的方法,考查了共固定化酶的动力学性质。试验结果表明:与溶液酶相比较,固定化蔗糖酶和GOD的响应滞迟期分别为3分钟和2分钟,4态响应时间增加6分钟和4分钟,Km值增大,pH─活力曲线变宽,最适pH值分别增大0.7和0.64,最适温度则降低7.3℃和16℃。以活性氧化铝作载体,戊二醛作交联剂制备的共固定化蔗糖酶和GOD,其蛋白质固定化率为92.9%,分解葡萄糖的总速度为441.6IU,当蔗糖浓度在0.2%以内时其反应速度与蔗糖浓度呈正相关(r=0.996),使用半衰期1623次,在4℃下保存120天活力残存为83.7%。
It was researched that a method of co-immobilized sucrase and GOD by adsorption and crosslinkog,the kinetics.Compared with liquid enzymes, Km value of the sucrase or GOD was more large, the pH active curve more wide, arid the optimum pH value increased 0. 7 or 0. 64 separately, but the optimum temperture conversely decreased 7. 3℃ or 16 ℃.Besides the stead/ resPOnse thee was extended six or four mins, respectively,the hysteresis thee of response was equal to three or two mins.A ratio of the immobilized protein in co-immobilized granula that was prepared with active alumina supporter and cross-link agent of glutaric dialdehyde, was equal to 62. 9 percent, total reactive speed about oxidizing glucose 441. 6IU and the half-life 1623 times respectively and the retention activity 83. 7 percent after stored three mothes at temperatUre below 4℃. The reactive speed was proprtional to sucrase concentration which was at below 0. 2 percent.
出处
《生物技术》
CAS
CSCD
1994年第2期10-13,共4页
Biotechnology