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以普通定性滤纸为底物 ,经碱处理后 ,研究其对纤维素酶的亲和吸附作用。结果表明 ,普通定性滤纸对纤维素酶具有比较强的特异性吸附作用 ,能够从粗酶液中分离出纤维素酶 ,再经POROS 2 0HQ阴离子交换柱纯化后即可得到电泳纯的纤维素酶。该法大大简化了传统的纤维素酶纯化工艺 ,所得的纤维素酶活力极高 ,比活达 35 0U/mg以上 ,滤纸一步吸附后纤维素酶的纯化倍数为 9 5 5 ,活性回收率在 10 %左右。纯化后的纤维素酶为内切 β 葡聚糖酶 ,相对分子质量为 6 0 0 0 0 ,最佳 pH为 4 0 ,最佳温度为 70℃。
The common qualitative filter paper as the substrate, after alkali treatment, to study its affinity for cellulase adsorption. The results showed that the common qualitative filter paper has a strong specific adsorption on cellulase, cellulase can be separated from the crude enzyme solution, and purified by POROS 20HQ anion exchange column to obtain electrophoretically pure cellulase . The method greatly simplifies the traditional cellulase purification process, the resulting cellulase activity is extremely high, the specific activity of 35 0U / mg or more, the filter paper after one-step adsorption of cellulase purification multiples of 9 5 5, the activity recovery in the About 10%. The purified cellulase was endo-β-glucanase, the molecular weight was 60,000, the optimum pH was 40 and the optimum temperature was 70 ℃.