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    Preparation of a Monolith with Covalently Bound Bovine Serum Albumin for Capillary Electrochromatography

    Access Status
    Fulltext not available
    Authors
    Yao, C.
    Tang, S.
    Yan, C.
    Yao, Hong Mei
    Tade, Moses
    Date
    2012
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Yao, 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.
    Source Title
    Analytical Letters
    DOI
    10.1080/00032719.2012.689793
    ISSN
    0003-2719
    School
    Department of Chemical Engineering
    URI
    http://hdl.handle.net/20.500.11937/42983
    Collection
    • Curtin Research Publications
    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.

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