Refolding kinetics of denatured-reduced lysozyme in the presence of folding aids
Refolding kinetics of denatured-reduced lysozyme in the presence of folding aids
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DOI：
10.1016/j.jbiotec.2004.06.012
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发表时间：
2004-10-19
影响因子：
4.1
通讯作者：
Sun, Y
中科院分区：
文献类型：
--
作者：
Dong, XY;Huang, Y;Sun, Y
利用一级折叠反应与三级聚集反应竞争的简化模型，研究了变性还原溶菌酶在折叠助剂（乙酰胺、丙酮、硫脲、L-精氨酸和甘油）存在下的复性动力学行为。发现蛋白质折叠助剂可分为两类。其中一种在适当的浓度下，如乙酰胺、丙酮、硫脲和L-精氨酸，稳定未折叠的蛋白质或折叠中间体。在这些添加剂的存在下，折叠速率随其浓度的增加而降低，并且存在一个浓度，其中聚集速率常数最小。因此，存在一个最佳浓度的折叠助剂，以产生高产量。另一组是蛋白质稳定剂，如甘油。在这类折叠助剂的存在下，提高其浓度到适当的值，可以提高复性速率和收率。此外，它们对改善蛋白质重折叠的效果是第一组的叠加。因此，两种折叠助剂的协同应用可获得较好的复性率和蛋白质得率。(C)2004 Elsevier B. V.保留所有权利。
The refolding kinetic behavior of denatured-reduced lysozyme in the presence of folding aids (acetamide, acetone, thiourea, L-arginine or glycerol) was studied utilizing a simplified model describing the competition between first-order folding reaction and third-order aggregation. It was found that the protein folding aids could be categorized into two groups. One of them at proper concentrations, such as acetamide, acetone, thiourea and L-arginine, stabilized unfolded protein or folding intermediates. In the presence of these additives, the folding rate decreased with increasing their concentration, and there existed a concentration where the aggregation rate constant was minimized. So, there was an optimum concentration for the folding aids to produce a high yield. The other group was protein stabilizers such as glycerol. In the presence of this kind of folding aids, both the refolding rate and yield were enhanced by increasing their concentration to a proper value. Moreover, their effect on improving protein refolding was additive to those of the first group. So the cooperative application of the two kinds of folding aids could result in favorable refolding rate and yield of protein. (C) 2004 Elsevier B.V. All rights reserved.