中文摘要：

进行了低酶液纯度的过氧化物酶快速结晶实验，经丙酮-硫酸铵协同沉淀纯化后，快速加入硫酸铵。得到了尺寸为40μm×30μm的晶体。活性检测证实，所得到的晶体为过氧化物酶晶体。结果表明，尽管酶溶液纯度不高，但当迅速达到过饱和时，仍然可以结晶，这与传统的蛋白质结晶过程明显不同。此外，研究了一种新的酶纯化工艺：丙酮-硫酸铵协同沉淀纯化，减少了操作步骤，提高了效率。

英文摘要：

Soybean hull peroxides （SHP） was crystallized with enzyme solution of low purity by the simple means of ＂fast crystallization method＂. After the enzyme solution was purified by acetone-ammonium sulfate cooperation precipitation, ammonium sulfate was quickly added to the enzyme solution. Then lumpy crystals with the size of about 40 ×30μm were obtained. The crystals were confirmed to be the SHP crystal through enzyme activity test. The result shows that though the purity of enzyme solution is not high, crystals can still be formed when the enzyme solution rapidly reaches to a degree of super saturation, which is different from the traditional methods of protein crystallization. Additionally, a novel purification method of ammonium sulfate-acetone cooperation precipitation was also studied. The new method can reduce the procedure and obtain a great efficiency.