Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/31595
Title: Application of Membrane Technologies for Biomolecules Separation and Purification by Affinity Binding to Specific Ligands
Authors: FELINIA
Keywords: Chiral separation, Affinity ultrafiltration, Reusability, Ionic strengh, Human serum albumin, Tryptophan
Issue Date: 10-Nov-2011
Source: FELINIA (2011-11-10). Application of Membrane Technologies for Biomolecules Separation and Purification by Affinity Binding to Specific Ligands. ScholarBank@NUS Repository.
Abstract: The reusability of human serum albumin (HSA) as a stereoselective ligand for D,L-tryptophan separation in the affinity ultrafiltration (UF) system has been demonstrated by readjusting the medium pH from an acidic to a basic condition. The native and recovered HSA molecules exhibit a similar D,L-tryptophan separation factor of 5-7 under the same experimental conditions. Moreover, a high recovery percentage of HSA above 80% has also been obtained by controlling both membrane pore size and hydrophilicity. The combination of these two features (HSA reusability and high recovery) is very helpful for the large-scale industrial application of the affinity UF system in chiral separation. Besides, it has been found that the HSA binding capability to L-tryptophan could be affected by the solution ionic strength. A higher solution ionic strength may result in a decrease in amounts of L-tryptophan bound to HSA due to the changes in solution environment and HSA structure.
URI: http://scholarbank.nus.edu.sg/handle/10635/31595
Appears in Collections:Master's Theses (Open)

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