Chiral separation of DL-tryptophan using porous membranes containing multilayered bovine serum albumin crosslinked with glutaraldehyde.
Bovine serum albumin (BSA) as a chiral ligand was captured uniformly throughout a porous hollow-fiber membrane at a level of 160 mg/g by the polymer chains grafted onto the membrane. BSA was bound in three layers with an end-on orientation to diethylamino groups on the graft chains which expanded from the pore surface towards the pore interior due to mutual electrostatic repulsion. Subsequently, crosslinking of BSA with a 0.025% (w/w) of glutaraldehyde in a Tris-HCl buffer (pH 8) for 4 h was effective in stabilizing the amount of BSA immobilized at a level of 150 mg/g. A solution of DL-tryptophan in a Tris-HCl buffer as a mobile phase permeated the crosslinked-BSA multilayered membrane and produced a chromatogram with a separation factor of 12. BSA leakage was not detected in the mobile phases at various pH values and organic modifiers.
Nakamura
M
M
Department of Specialty Materials, Faculty of Engineering, Chiba University, Japan.
Kiyohara
S
S
Saito
K
K
Sugita
K
K
Sugo
T
T
D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D003432:Cross-Linking Reagents; D005976:Glutaral / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D008567:Membranes, Artificial; D012710:Serum Albumin, Bovine / Q000032:analysis*; D013237:Stereoisomerism; D014364:Tryptophan / Q000302:isolation & purification*
D003432:Cross-Linking Reagents; D008567:Membranes, Artificial; D012710:Serum Albumin, Bovine; D014364:Tryptophan; D005976:Glutaral