A Study of Ion-Exchange Chromatography in an Expanded Bed for Bovine Albumin Recovery

被引：4
|
作者：
Severo, Joao Batista, Jr. [2 ]
de Souza, Roberto Rodrigues [2 ]
Curvelo Santana, Jose Carlos [1 ]
Tambourgi, Elias Basile [1 ]
机构：
[1] Univ Estadual Campinas, Fac Engn Quim, BR-13083970 Campinas, SP, Brazil
[2] Univ Fed Sergipe, Dept Engn Quim, BR-49100000 Sao Cristovao, SE, Brazil
来源：
BRAZILIAN ARCHIVES OF BIOLOGY AND TECHNOLOGY | 2009年 / 52卷 / 02期
关键词：
BSA; protein adsorption; breakthrough curves; Amberlite IRA 410 ion-exchange resin; distribution residence time study; Richardson-Zack coefficient; ZEA-MAYS MALT; OPTIMIZATION; ADSORPTION; AMYLASES;
D O I：
10.1590/S1516-89132009000200021
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
In the present work, the effect of bed expansion on BSA adsorption on Amberlite IRA 410 ion-exchange resin was studied. The hydrodynamic behavior of an expanded bed adsorption column on effects of the biomolecules and salt addition and temperature were studied to optimize the conditions for BSA recovery on ion-exchange resin. Residence time distribution showed that HEPT, axial dispersion and the Pecletl number increased with temperature and bed height, bed voidage and linear velocity. The binding capacity of the resin increased with bed height. The Amberlite IRA 410 ion-exchange showed an affinity for BSA with a recovery yield of 78.36 % of total protein.
引用
收藏
页码：427 / 436
页数：10
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