【摘要】 将提纯的一种内切型肝素酶固定于聚酯载体上 ,固定化效率达 78 8%。酶活力在pH为 7 5左右时表现最高 ,并且在此条件下固定化酶的稳定性最好。最适反应温度为 4 0℃。热稳定性试验表明 ,固定化酶的稳定性较差。固定化酶的使用半衰期比游离酶延长 4 4倍。固定化酶催化肝素底物反应的Km 值约为 95 4 μmol L而游离酶的Km 值约为 71 2 μmol L。固定化酶可以同时作用于肝素和硫酸乙酰肝素 ,而对硫酸软骨素没有催化能力。肝素经降解后 ,产生一定量的非硫酸化或低硫酸化的二糖和不同聚合度的寡糖混合物。更多还原

【Abstract】 A purified heparinase from the species of Sphingobacterium was immobilized on the polyether carrier with the recovery of 78.8%. The immobilized enzyme showed highest activity under pH 7.5, more stability around pH7.0. Its optimal temperature was 40℃, but thermostability was poor. Half life of the immobilized heparinase prolonged by 4.4 times than free heparinase. The Michaelis constant of the immobilized heparinase for heparin was 95.4μmol/L, and that of free heparinase was 71.2μmol/L. Heparin and heparan sulfate were both suit substrates of the enzyme. The mixture of heparin oligosaccharides degraded by immobilized heparinase contained both low sulfated disaccharides and more other oligosaccharides with different polymerization.更多还原