Enzyme immobilization in a biomimetic silica support
Enzyme immobilization in a biomimetic silica support
复制标题
DOI：
10.1038/nbt931
复制
发表时间：
2004-02-01
影响因子：
46.9
通讯作者：
Stone, MO
中科院分区：
文献类型：
--
作者：
Luckarift, HR;Spain, JC;Stone, MO
保持生物分子活性的稳健固定化技术具有许多潜在应用（1-8）。硅酸盐，主要以溶胶-凝胶复合材料或功能化介孔二氧化硅的形式，已被用于封装各种生物分子（1，4 -8），但化学合成所需的苛刻条件限制了其适用性（1，8）。来自硅藻的Silaffin多肽在中性pH和环境温度和压力下体外催化二氧化硅的形成（9）。在这里，我们表明，丁酰胆碱酯酶截留在沉淀的二氧化硅纳米球保留其所有的活动。90%的可溶性酶被固定化，并且固定化酶比游离酶稳定得多。二氧化硅纳米球的机械性能促进了在流通式反应器中的应用。生物二氧化硅用于酶固定化结合了二氧化硅基质的优异支持特性和保持酶活性的良性固定化方法。
Robust immobilization techniques that preserve the activity of biomolecules have many potential applications(1-8). Silicates, primarily in the form of sol-gel composites or functionalized mesoporous silica, have been used to encapsulate a wide variety of biomolecules(1,4-8) but the harsh conditions required for chemical synthesis limit their applicability(1,8). Silaffin polypeptides from diatoms catalyze the formation of silica in vitro at neutral pH and ambient temperature and pressure(9). Here we show that butyrylcholinesterase entrapped during the precipitation of silica nanospheres retained all of its activity. Ninety percent of the soluble enzyme was immobilized, and the immobilized enzyme was substantially more stable than the free enzyme. The mechanical properties of silica nanospheres facilitated application in a flow-through reactor. The use of biosilica for enzyme immobilization combines the excellent support properties of a silica matrix with a benign immobilization method that retains enzyme activity.