DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Suhyeok | - |
dc.contributor.author | Joo, Kye Il | - |
dc.contributor.author | Jo, Byung Hoon | - |
dc.contributor.author | Cha, Hyung Joon | - |
dc.date.accessioned | 2021-12-03T09:24:46Z | - |
dc.date.available | 2021-12-03T09:24:46Z | - |
dc.date.created | 2020-07-14 | - |
dc.date.issued | 2020-06 | - |
dc.identifier.issn | 1944-8244 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/107881 | - |
dc.description.abstract | Exploiting carbonic anhydrase (CA), an enzyme that catalyzes the hydration of CO2, is a powerful route for ecofriendly and cost-effective carbon capture and utilization. For successful industrial applications, the stability and reusability of CA should be improved, which necessitates enzyme immobilization. Herein, the ribosomal protein L2 (Si-tag) from Escherichia coli was utilized for the immobilization of CA onto diatom biosilica, a promising renewable support material. The Si-tag was redesigned (L2NC) and genetically fused to CA from the marine bacterium Hydrogenovibrio marinus (hmCA). One-step self-immobilization of hmCA-L2NC onto diatom biosilica by simple mixing was successfully achieved via Si-tag-mediated strong binding, showing multilayer adsorption with a maximal loading of 1.4 wt %. The immobilized enzyme showed high reusability and no enzyme leakage even under high temperature conditions. The activity of hmCA-L2NC was inversely proportional to the enzyme loading, while the stability was directly proportional to the enzyme loading. This discovered activity-stability trade-off phenomenon could be attributed to macromolecular crowding on the highly dense surface of the enzyme-immobilized biosilica. Collectively, our system not only facilitates the stability-controllable self-immobilization of enzyme via Si-tag on a diatom biosilica support for the robust, facile, and green construction of stable biocatalysts, but is also a unique model for studying the macromolecular crowding effect on surface-immobilized enzymes. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.relation.isPartOf | ACS APPLIED MATERIALS & INTERFACES | - |
dc.title | Stability-Controllable Self-Immobilization of Carbonic Anhydrase Fused with a Silica-Binding Tag onto Diatom Biosilica for Enzymatic CO2 Capture and Utilization | - |
dc.type | Article | - |
dc.identifier.doi | 10.1021/acsami.0c03804 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | ACS APPLIED MATERIALS & INTERFACES, v.12, no.24, pp.27055 - 27063 | - |
dc.identifier.wosid | 000542925300027 | - |
dc.citation.endPage | 27063 | - |
dc.citation.number | 24 | - |
dc.citation.startPage | 27055 | - |
dc.citation.title | ACS APPLIED MATERIALS & INTERFACES | - |
dc.citation.volume | 12 | - |
dc.contributor.affiliatedAuthor | Kim, Suhyeok | - |
dc.contributor.affiliatedAuthor | Joo, Kye Il | - |
dc.contributor.affiliatedAuthor | Cha, Hyung Joon | - |
dc.identifier.scopusid | 2-s2.0-85086681799 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | SI-TAG | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | DIOXIDE | - |
dc.subject.keywordPlus | BIOCATALYST | - |
dc.subject.keywordPlus | ADSORPTION | - |
dc.subject.keywordPlus | CONVERSION | - |
dc.subject.keywordPlus | ENZYMES | - |
dc.subject.keywordPlus | LIPASES | - |
dc.subject.keywordPlus | SURFACE | - |
dc.subject.keywordPlus | CELITE | - |
dc.subject.keywordAuthor | carbonic anhydrase | - |
dc.subject.keywordAuthor | silica-binding tag | - |
dc.subject.keywordAuthor | biosilica | - |
dc.subject.keywordAuthor | Hydrogenovibrio marinus | - |
dc.subject.keywordAuthor | enzyme immobilization | - |
dc.subject.keywordAuthor | mactomolecular crowding | - |
dc.relation.journalWebOfScienceCategory | Nanoscience & Nanotechnology | - |
dc.relation.journalWebOfScienceCategory | Materials Science, Multidisciplinary | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalResearchArea | Materials Science | - |
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