Optimization of the enantiomeric separation of tryptophan analogs by membrane processes

摘要

The separation of racemic tryptophan analogs has been performed by two ways: ultrafiltration in a solution system using bovine serum albumin (BSA) as a free chiral selector and dialysis using BSA grafted nylon membrane. A complexation mechanism based on competitive binding of both D- and L-tryptophan zwitter-ionic form on the same unprotonated protein site has been used to predict recovery and purity of both D- and L-tryptophan in the retentate and permeate.