摘要
从青霉菌m8提取出木聚糖酶，将其固定在用戊二醛交联的壳聚糖载体上。1．0g壳聚糖与4％的二醛结合固定3．5mg蛋白，酶活回收率为46．6％。在酶的最适pH为4．6，固定化酶为pH3．8。原酶的最适温度为55℃，固定化酶在60－75℃都具有较高活性。固定化酶的耐热性优于原酶，固定化酶的表现Km值略低于原酶，前者为5．0×10－2g／L，后者为3．58×10－2g／L。
The extracellular xylanase from Peaicillium was immobilized on chitosan by glutaraldehyde.The results indicated that the immobilized-xylanase prepared by 1. 0g chitosan crosslinking with4% glutaralhyde and then combining with 3. 5mg enzyme showed higher enzyme activity and better activity recoveries(46. 6 % ). The optimum pH of soluble enzyme and temperature of solubleenzyme was 55℃, wherease immobilized enzyme showed high activity in 60 - 75℃. The thermalstability of immobilized enzyme was better than soluble enzyme at 65℃. The apparent Km' ofthe immobilized enzyme was 3. 58 ×10 -2g/L and the substrate.
出处
《生物技术》
CAS
CSCD
1999年第5期15-18,共4页
Biotechnology
基金
山东省科委科研资金!971164805
