| Abstract
| - A novel protein-encapsulation technique using sol−gelswas developed for the preparation of monolithic capillarycolumns for capillary electrochromatography. Two chiralcompounds, bovine serum albumin (BSA) and ovomucoid(OVM) from chicken egg white, were encapsulated intetramethoxysilane-based hydrogel and their chiral selectivity was evaluated for the separation of some selectedenantiomers (tryptophan, benzoin, eperisone, chlorpheniramine). The protein encapsulation was carried outwithin a capillary in a single step under mild conditions.The resultant monolithic columns showed adequate chromatographic performance, including mechanical strength,penetration of pressurized flow, and chiral separation.Two different proteins, BSA and OVM, were successfullyencapsulated into the gel matrixes by changing the alkoxysilane compositions of the gel. Run-to-run repeatabilitywas quite satisfactory. The consecutive analysis of theneutral compound, benzoin, by the OVM-encapsulatedcolumn showed good repeatability in the retention time(RSD = 1.23% for the first peak, N = 10). Underoptimized conditions, the theoretical plate number for thefirst peak of benzoin reached 72 000 plates/m.
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