Characterization of protein adsorption by composite silica-polyacrylamide gel anion exchangers .1. Equilibrium and mass transfer in agitated contactors

Characterization of protein adsorption by composite silica-polyacrylamide gel anion exchangers .1. Equilibrium and mass transfer in agitated contactors
复制标题

DOI:
10.1016/0021-9673(96)00337-8
复制
发表时间:
1996-10-11
影响因子:
4.1
通讯作者:
Carta, G
Carta, G
中科院分区:
化学2区
文献类型:
--
作者:
Fernandez, MA;Carta, G

文献摘要

被引文献

相似文献

研究了商品名为HyperD的复合多孔二氧化硅-聚丙烯酰胺凝胶离子交换剂对蛋白质的吸收。这些离子交换剂具有极高的静态吸附容量,大于约200 mg/cm(3),并具有快速的吸附动力学。它们的机械强度很高,适合在流动相流速较高的情况下进行层析。通过实验获得了这些离子交换剂对蛋白质的吸收平衡,发现它们遵循质量作用定律。因此,通过改变溶液离子强度,可以实现蛋白质的可逆吸附和解吸。在适宜的吸收条件下,还得到了搅拌接触器中的间歇传质速率。当蛋白质浓度较低时,吸收动力学受液相传质阻力控制,当蛋白质浓度较高时,吸收动力学受颗粒内传质阻力控制。在后一种情况下,吸收很快,在5-10分钟内可获得直径49-76微米的几乎完全饱和。通过将实验结果与模型预测进行比较,得到了描述这些离子交换器间歇吸附动力学的模型参数。
The uptake of proteins by composite porous silica-polyacrylamide gel ion exchangers known under the trade name HyperD, is investigated. These ion exchangers are found to have an exceptionally high static adsorption capacity, greater than about 200 mg/cm(3), and a rapid uptake kinetics. Being mechanically quite strong, they are suitable for chromatography applications at elevated mobile phase flow-rates. The uptake equilibrium of proteins by these ion exchangers is obtained experimentally and is found to follow the mass action law. Thus, reversible adsorption and desorption of proteins is obtained by varying the solution ionic strength. Batch mass transfer rates in an agitated contactor under favorable uptake conditions are also obtained. The uptake kinetics is controlled by the fluid phase mass transfer resistance for low protein concentrations, and by the intraparticle mass transfer resistance at high protein concentrations. In the latter case, the uptake is quite rapid and nearly complete saturation of particles 49-76 mu m in diameter can be obtained in 5 to 10 min. The parameters of a model describing the batch uptake kinetics in these ion exchangers are obtained by comparing experimental results with model predictions.