Protein recovery from surfactant precipitation
Protein recovery from surfactant precipitation
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DOI：
10.1002/btpr.671
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发表时间：
2011-11
影响因子：
2.9
通讯作者：
S. Cheng;D. Stuckey
中科院分区：
文献类型：
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作者：
S. Cheng;D. Stuckey
使用两种溶剂和反离子表面活性剂研究了从含有沉淀的溶菌酶-AOT复合物的水溶液中回收溶菌酶，所述沉淀的溶菌酶-AOT复合物通过将双-（2-乙基己基）磺基琥珀酸钠（AOT）直接添加到溶菌酶溶液中而形成。乙醇、甲醇和溶剂混合物溶解表面活性剂沉淀物并回收固体形式的溶菌酶。回收率和蛋白质稳定性随所用溶剂的类型而变化。还使用反离子表面活性剂：三辛基甲基氯化铵（TOMAC）评价了一种完全不同的回收方法，所述反离子表面活性剂与AOT结合，将溶菌酶释放到溶液中。在2：1（TOMAC：AOT）的摩尔比下实现了溶菌酶的完全回收（100%），并且在最终水相中保持了原始蛋白质活性。回收的溶菌酶保留其二级结构中观察到的圆二色性（CD）光谱。比活性研究表明，反离子表面活性剂提取不改变酶的生物活性。© 2011美国化学工程师学会生物技术。程序，，2011
The recovery of lysozyme from an aqueous solution containing precipitated lysozyme‐AOT complexes formed by the direct addition of sodium bis‐(2‐ethylhexyl) sulfosuccinate (AOT) to a lysozyme solution was studied using both solvents, and a counterionic surfactant. Ethanol, methanol and solvent mixtures dissolved the surfactant precipitate and recovered lysozyme as a solid. Recovery efficiency and protein stability varied with the type of solvent used. An entirely different method of recovery was also evaluated using a counterionic surfactant: trioctylmethylammonium chloride (TOMAC) which bound to AOT releasing lysozyme into solution. Complete recovery (100%) of lysozyme was achieved at a molar ratio of 2:1 (TOMAC:AOT), and the original protein activity was maintained in the final aqueous phase. The recovered lysozyme retained its secondary structure as observed in circular dichroism (CD) spectra. Specific activity studies show that counterionic surfactant extraction does not alter the biological activity of the enzyme. © 2011 American Institute of Chemical Engineers Biotechnol. Prog.,, 2011