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|Title:||Iron oxide filled magnetic carbon nanotube-enzyme conjugates for recycling of amyloglucosidase: Toward useful applications in biofuel production process||Authors:||Goh, W.J.
|Issue Date:||11-Dec-2012||Citation:||Goh, W.J., Makam, V.S., Hu, J., Kang, L., Zheng, M., Yoong, S.L., Udalagama, C.N.B., Pastorin, G. (2012-12-11). Iron oxide filled magnetic carbon nanotube-enzyme conjugates for recycling of amyloglucosidase: Toward useful applications in biofuel production process. Langmuir 28 (49) : 16864-16873. ScholarBank@NUS Repository. https://doi.org/10.1021/la303046m||Abstract:||Biofuels are fast advancing as a new research area to provide alternative sources of sustainable and clean energy. Recent advances in nanotechnology have sought to improve the efficiency of biofuel production, enhancing energy security. In this study, we have incorporated iron oxide nanoparticles into single-walled carbon nanotubes (SWCNTs) to produce magnetic single-walled carbon nanotubes (mSWCNTs). Our objective is to bridge both nanotechnology and biofuel production by immobilizing the enzyme, Amyloglucosidase (AMG), onto mSWCNTs using physical adsorption and covalent immobilization, with the aim of recycling the immobilized enzyme, toward useful applications in biofuel production processes. We have demonstrated that the enzyme retains a certain percentage of its catalytic efficiency (up to 40%) in starch prototype biomass hydrolysis when used repeatedly (up to ten cycles) after immobilization on mSWCNTs, since the nanotubes can be easily separated from the reaction mixture using a simple magnet. The enzyme loading, activity, and structural changes after immobilization onto mSWCNTs were also studied. In addition, we have demonstrated that the immobilized enzyme retains its activity when stored at 4 C for at least one month. These results, combined with the unique intrinsic properties of the nanotubes, pave the way for greater efficiency in carbon nanotube-enzyme bioreactors and reduced capital costs in industrial enzyme systems. © 2012 American Chemical Society.||Source Title:||Langmuir||URI:||http://scholarbank.nus.edu.sg/handle/10635/97004||ISSN:||07437463||DOI:||10.1021/la303046m|
|Appears in Collections:||Staff Publications|
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