Lysozyme-magnesium aluminum silicate microparticles: Molecular interaction, bioactivity and release studies

Watchara Kanjanakawinkul, Natalie J. Medlicott, Thomas Rades, Satit Puttipipatkhachorn, Thaned Pongjanyakul

    6 Citations (Scopus)

    Abstract

    The objectives of this study were to investigate the adsorption behavior of lysozyme (LSZ) onto magnesium aluminum silicate (MAS) at various pHs and to characterize the LSZ–MAS microparticles obtained from the molecular interaction between LSZ and MAS. The results showed that LSZ could be bound onto the MAS layers at different pHs, leading to the formation of LSZ–MAS microparticles. The higher preparation pH permitted greater adsorption affinity but a lower adsorption capacity of LSZ onto MAS. LSZ could interact with MAS via hydrogen bonds and electrostatic forces, resulting in the formation of intercalated nanocomposites. The particle size, %LSZ adsorbed, and LSZ release rate of LSZ–MAS microparticles increased when the LSZ–MAS ratio was increased. The secondary structure of LSZ bound onto the MAS layers in microparticles prepared at various pHs was altered compared with that of native LSZ. Moreover, the LSZ extracted from microparticles prepared at pH 4 showed an obvious change in the tertiary structure, leading to a decrease in the biological activity of the LSZ released. These findings suggested that LSZ can strongly interact with MAS to form microparticles that may potentially be used as delivery systems for sustained protein release.
    Original languageEnglish
    JournalInternational Journal of Biological Macromolecules
    Volume80
    Pages (from-to)651-658
    Number of pages8
    ISSN0141-8130
    DOIs
    Publication statusPublished - 1 Sept 2015

    Keywords

    • Lysozyme
    • Magnesium aluminum silicate
    • Microparticles
    • Protein conformation
    • Bioactivity
    • Protein release

    Fingerprint

    Dive into the research topics of 'Lysozyme-magnesium aluminum silicate microparticles: Molecular interaction, bioactivity and release studies'. Together they form a unique fingerprint.

    Cite this