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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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.[1]

References

  1. Chiral separation of DL-tryptophan using porous membranes containing multilayered bovine serum albumin crosslinked with glutaraldehyde. Nakamura, M., Kiyohara, S., Saito, K., Sugita, K., Sugo, T. Journal of chromatography. A. (1998) [Pubmed]
 
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