Enzyme Immobilisation on Amino-Functionalised Multi-Walled Carbon Nanotubes: Structural and Biocatalytic Characterisation

Madan Verma, Minoo Naebe, Colin Barrow, Munish Puri

    Research output: Contribution to journalArticlepeer-review

    122 Citations (Scopus)


    Background:The aim of this work is to investigate the structure and function of enzymes immobilised on nanomaterials. This work will allow better understanding of enzyme-nanomaterial interactions, as well as designing functional protein-nanomaterial conjugates.Methodology/Principal Findings:Multiwalled carbon nanotubes (MWNTs) were functionalised with amino groups to improve solubility and biocompatibility. The pristine and functionalised forms of MWNTs were characterised with Fourier-transform infrared spectroscopy. Thermogravimetric analysis was done to examine the degree of the functionalisation process. An immobilised biocatalyst was prepared on functionalised nanomaterial by covalent binding. Thermomyces lanuginosus lipase was used as a model enzyme. The structural change of the immobilised and free lipases were characterised with transmission electron Microscopy, X-ray photoelectron spectroscopy, Fourier-transform infrared spectroscopy and Circular dichroism spectroscopy. Biochemical characterisation of immobilised enzyme showed broader pH and thermal optima compared to soluble form. Reusability of the immobilised enzyme for hydrolysis of long chain esters was demonstrated up to ten cycles.Conclusion/Significance:Lipase immobilised on MWNTs has exhibited significantly improved thermal stability. The exploration of advanced nanomaterial for enzyme immobilisation support using sophisticated techniques makes nanobiocatalyst of potential interest for biosensor applications.

    Original languageEnglish
    Article numbere73642
    Pages (from-to)Art: e73642
    Number of pages9
    JournalPLoS One
    Issue number9
    Publication statusPublished - 12 Sep 2013


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