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dc.contributor.authorYao, C.
dc.contributor.authorTang, S.
dc.contributor.authorYan, C.
dc.contributor.authorYao, Hong Mei
dc.contributor.authorTade, Moses
dc.date.accessioned2017-01-30T15:03:37Z
dc.date.available2017-01-30T15:03:37Z
dc.date.created2015-03-03T20:16:36Z
dc.date.issued2012
dc.identifier.citationYao, C. and Tang, S. and Yan, C. and Yao, H.M. and Tade, M. 2012. Preparation of a Monolith with Covalently Bound Bovine Serum Albumin for Capillary Electrochromatography. Analytical Letters. 45 (16): pp. 2377-2388.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/42983
dc.identifier.doi10.1080/00032719.2012.689793
dc.description.abstract

Capillary electrochromatography (CEC) is important for applications in enantiomer separation. The problems associated with column fabrication bring a challenge in developing monoliths with ease of preparation, robustness of separation, enhanced mass transfer, and lower pressure drop. In this research, the covalent binding of proteins on to a monolithic matrix was investigated to overcome the drawback of loss and/or denaturing of the biomolecules from physical adsorption and encapsulation method. A chitosan/silica hybrid monolith was prepared and a protein, bovine serum albumin, was covalently immobilized on the column. The prepared monolith was evaluated using the enantioseparation of D,L-tryptophan by CEC. It was found that separation of tryptophan enantiomers with a resolution of 2.44 was achieved by using 20 mmolL-1 phosphate buffer at pH 7.5. A higherchitosan concentration was also proven to be of possible use in the synthesis with the aid of acetic acid as the solvent. The much shorter retention time and increased separation ability demonstrate the advantages of capillary column under investigation.

dc.publisherTaylor & Francis Inc.
dc.subjectEnantioseparation
dc.subjectBovine serum albumin
dc.subjectChitosan
dc.subjectCapillary electrochromatography
dc.subjectMonolith
dc.titlePreparation of a Monolith with Covalently Bound Bovine Serum Albumin for Capillary Electrochromatography
dc.typeJournal Article
dcterms.source.volume45
dcterms.source.startPage2377
dcterms.source.endPage2388
dcterms.source.issn0003-2719
dcterms.source.titleAnalytical Letters
curtin.departmentDepartment of Chemical Engineering
curtin.accessStatusFulltext not available


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