Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Justyn Wayne Jaworski | - |
dc.date.accessioned | 2018-03-14T07:16:56Z | - |
dc.date.available | 2018-03-14T07:16:56Z | - |
dc.date.issued | 2014-06 | - |
dc.identifier.citation | COLLOIDS AND SURFACES B-BIOINTERFACES, 권: 122, 페이지: 846-850 | en_US |
dc.identifier.issn | 0927-7765 | - |
dc.identifier.issn | 1873-4367 | - |
dc.identifier.uri | http://www.sciencedirect.com/science/article/pii/S0927776514004329?via%3Dihub | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11754/46756 | - |
dc.description.abstract | The covalent immobilization of proteins onto surfaces is an essential aspect of several fields of research, including proteomics, sensing, heterogeneous biocatalysis, and more broadly biotechnology. Site-specific, covalent attachment of proteins has been achieved in recent years by the use of expanded genetic codes to produce proteins with controlled placement of un-natural amino acids bearing bio-orthogonal functional groups. Unfortunately, the complexity of developing such systems is impractical for most laboratories; hence, a less complicated approach to generating un-natural amino acid side-chains has been employed. Utilizing a straightforward reaction with formylglycine generating enzyme, we use the site-specific modification of engineered proteins to yield un-natural amino acid side-chains for protein immobilization. Using this approach, we demonstrate the controlled immobilization of various enzymes onto a variety of amine coated surfaces. Our results reveal reusability of the immobilized enzymes via this strategy, and furthermore, we find the activity of the immobilized enzymes to remain even after a month of use indicating significant stability of the linkage. (c) 2014 Elsevier B.V. All rights reserved. | en_US |
dc.description.sponsorship | This work was supported by the Basic Science Research Program through the National Research Foundation (NRF) funded by the Ministry of Science, ICT & Future Planning (2013R1A1A1076117) and also by the Priority Research Centers Program through the NRF funded by the Ministry of Education (2012R1A6A1029029). Further support was provided by the research fund of Hanyang University (HY-2012-N). | en_US |
dc.language.iso | en | en_US |
dc.publisher | ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS | en_US |
dc.subject | Un-natural side chains | en_US |
dc.subject | Formylglycine generating enzyme | en_US |
dc.subject | Heterogeneous biocatalysis | en_US |
dc.subject | Surface modification | en_US |
dc.subject | Covalent attachment | en_US |
dc.subject | Site-specific linkage | en_US |
dc.title | Enzyme directed formation of un-natural side-chains for covalent surface attachment of proteins | en_US |
dc.type | Article | en_US |
dc.relation.volume | 122 | - |
dc.identifier.doi | 10.1016/j.colsurfb.2014.08.010 | - |
dc.relation.page | 846-850 | - |
dc.relation.journal | COLLOIDS AND SURFACES B-BIOINTERFACES | - |
dc.contributor.googleauthor | Cho, Hwa-young | - |
dc.contributor.googleauthor | Jaworski, Justyn | - |
dc.relation.code | 2014027563 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF ENGINEERING[S] | - |
dc.sector.department | DEPARTMENT OF CHEMICAL ENGINEERING | - |
dc.identifier.pid | justynj | - |
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