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Recyclable Cellulose-Containing Magnetic Nanoparticles: Immobilization of Cellulose-Binding Module-Tagged Proteins and Synthetic Metabolon Featuring Substrate Channeling

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dc.contributorVirginia Tech. Department of Biological Systems Engineeringen
dc.contributorVirginia Tech. Institute for Critical Technology and Applied Science (ICTAS)en
dc.contributorCell Free Bioinnovations Inc.en
dc.contributorGate Fuels Inc.en
dc.contributor.authorMyung, Suwanen
dc.contributor.authorYou, Chunen
dc.contributor.authorZhang, Y. H. Percivalen
dc.contributor.departmentBiological Systems Engineeringen
dc.date.accessed2015-04-17en
dc.date.accessioned2015-04-20T21:22:16Zen
dc.date.available2015-04-20T21:22:16Zen
dc.date.issued2013-07-01en
dc.description.abstractEasily recyclable cellulose-containing magnetic nanoparticles were developed for immobilizing family 3 cellulose-binding module (CBM)-tagged enzymes/proteins and a self-assembled three-enzyme complex called the synthetic metabolon. Avicel (microcrystalline cellulose)-containing magnetic nanoparticles (A-MNPs) and two controls of dextran-containing magnetic nanoparticles (D-MNPs) and magnetic nanoparticles (MNPs) were prepared by a solvothermal method. Their adsorption ability was investigated by using CBM-tagged green fluorescence protein and phosphoglucose isomerase. A-MNPs had higher adsorption capacity and tighter binding on CBM-tagged proteins than the two control MNPs because of the high-affinity adsorption of CBM on cellulose. In addition, A-MNPs were used to purify and co-immobilize a three-enzyme metabolon through a CBM-tagged scaffoldin containing three different cohesins. The three-enzyme metabolon comprised of dockerin-containing triosephosphate isomerase, aldolase, and fructose 1,6-bisphosphatase was self-assembled because of the high-affinity interaction between cohesins and dockerins. Thanks to spatial organization of the three-enzyme metabolon on the surface of A-MNPs, the metabolon exhibited a 4.6 times higher initial reaction rate than the non-complexed three-enzyme mixture at the same enzyme loading. These results suggested that the cellulose-containing MNPs were new supports for immobilizing enzymes, which could be selectively recycled or removed from other biocatalysts by a magnetic force, and the use of enzymes immobilized on A-MNPs could be very useful to control the On/Off process in enzymatic cascade reactions.en
dc.description.sponsorshipVirginia Tech. Department of Biological Systems Engineeringen
dc.description.sponsorshipShell. GameChanger Programen
dc.description.sponsorshipVirginia Tech. College of Agriculture and Life Sciences. Biodesign and Bioprocessing Research Centeren
dc.format.mimetypeapplication/pdfen
dc.identifier.citationMyung, S., You, C., & Zhang, Y. H. P. (2013). Recyclable cellulose-containing magnetic nanoparticles: immobilization of cellulose-binding module-tagged proteins and a synthetic metabolon featuring substrate channeling. Journal of Materials Chemistry B, 1(35), 4419-4427. doi: 10.1039/C3TB20482Ken
dc.identifier.doihttps://doi.org/10.1039/C3TB20482Ken
dc.identifier.issn2050-750Xen
dc.identifier.urihttp://hdl.handle.net/10919/51711en
dc.identifier.urlhttp://pubs.rsc.org/en/content/articlelanding/2013/tb/c3tb20482ken
dc.language.isoenen
dc.publisherThe Royal Society of Chemistryen
dc.rightsCreative Commons Attribution-NonCommercial 3.0 Unporteden
dc.rights.urihttp://creativecommons.org/licenses/by-nc/3.0/en
dc.subjectMagnetic nanoparticlesen
dc.subjectEnzyme immobilizationen
dc.subjectCellulose-binding module (CBM) tagsen
dc.titleRecyclable Cellulose-Containing Magnetic Nanoparticles: Immobilization of Cellulose-Binding Module-Tagged Proteins and Synthetic Metabolon Featuring Substrate Channelingen
dc.title.serialJournal of Materials Chemistry Ben
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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