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dc.contributor.authorEker, Bilge
dc.contributor.authorAsuri, Prashanth
dc.contributor.authorMurugesan, Saravanababu
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorDordick, Jonathan S.
dc.date2007
dc.date.accessioned2022-06-27T16:11:45Z
dc.date.available2022-06-27T16:11:45Z
dc.date.issued2007-11-01
dc.identifier.citationEnzyme-Carbon Nanotube Conjugates in Room Temperature Ionic Liquids, B. Eker, P. Asuri, S. Murugesan, R. J. Linhardt, J. S. Dordick, Applied Biochemistry and Biotechnology, 143, 153-163, 2007.
dc.identifier.issn2732289
dc.identifier.urihttps://doi.org/10.1007/s12010-007-0035-2
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5763
dc.descriptionApplied Biochemistry and Biotechnology, 143, 153-163
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractRoom-temperature ionic liquids (RTILs) are intriguing solvents, which are recognized as "green" alternatives to volatile organics. Although RTILs are nonvolatile and can dissolve a wide range of charged, polar, and nonpolar organic and inorganic molecules, there remain substantial challenges in their use, not the least of which is the solvents' high viscosity that leads to potential mass transfer limitations. In the course of this work, we discovered that the simple adsorption of the bacterial protease, proteinase K, onto single-walled carbon nanotubes (SWNTs) results in intrinsically high catalytic turnover. The high surface area and the nanoscopic dimensions of SWNTs offered high enzyme loading and low mass transfer resistance. Furthermore, the enzyme-SWNT conjugates displayed enhanced thermal stability in RTILs over the native suspended enzyme counterpart and allowed facile reuse. These enzyme-SWNT conjugates may therefore provide a way to overcome key operational limitations of RTIL systems.
dc.description.sponsorshipNational Science Foundation
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1007/s12010-007-0035-2
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofApplied Biochemistry and Biotechnology
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleEnzyme-Carbon Nanotube Conjugates in Room Temperature Ionic Liquids
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1007/s12010-007-0035-2
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1007/s12010-007-0035-2
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages153-163
rpi.description.volume143


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