Enantiomeric separation by ultrafiltration: complexation mechanism of tryptophan analogs to bovine serum albumin

被引：30

作者：

Garnier, F ^{[1
]}

Randon, J ^{[1
]}

Rocca, JL ^{[1
]}

机构：

[1] Univ Lyon 1, CNRS UMR 5619, Analyt Sci Lab, F-69622 Villeurbanne, France

来源：

SEPARATION AND PURIFICATION TECHNOLOGY | 1999年 / 16卷 / 03期

关键词：

BSA; complexation mechanism; enantiomeric separation; kynurenine; tryptophan;

D O I：

10.1016/S1383-5866(99)00017-9

中图分类号：

TQ [化学工业];

学科分类号：

0817 ;

摘要：

The separation of racemic tryptophan and its analogs can be performed by ultrafiltration in a solution system using bovine serum albumin (BSA) as a complexing agent. Three models have been tested to simulate the complexation mechanism of tryptophan and kynurenine enantiomers to BSA protein. In the pH range from 7 to 11, the most probable complexation mechanism was a competitive binding of D- and L-enantiomers on a single site. Based on these results the enantiomeric separation of these amino acids can be optimized in order to improve the selectivity and recovery of the BSA solution process. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：243 / 250

页数：8

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