Protein-inorganic hybrid system for efficient his-tagged enzymes immobilization and its application in L-xylulose production
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Patel, Sanjay K. S. | - |
dc.contributor.author | Otari, Sachin V. | - |
dc.contributor.author | Kang, Yun Chan | - |
dc.contributor.author | Lee, Jung-Kul | - |
dc.date.accessioned | 2021-09-03T15:29:34Z | - |
dc.date.available | 2021-09-03T15:29:34Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2017 | - |
dc.identifier.issn | 2046-2069 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/86478 | - |
dc.description.abstract | The facile synthesis of protein-inorganic hybrid nanoflowers was evaluated for the efficient immobilization of recombinant his-tagged enzymes, which have a broad range of potential applications. In this study, we report the preparation of a metal-protein hybrid nanoflower system for efficient immobilization of the recombinant enzymes L-arabinitol 4-dehydrogenase from Hypocrea jecorina (HjLAD) and NADH oxidase from Streptococcus pyogenes (SpNox). Compared with free enzymes, synthesized hybrid nanoflowers exhibited enhanced enzymatic activities of 246 and 144% for HjLAD and SpNox, respectively. We have demonstrated that immobilized enzymes retained high catalytic activity and improved the tolerance towards pH and temperature changes. Synthesized nanoflowers also retained high storage stability and reusability. In addition, the immobilized enzymes exhibited significantly enhanced L-xylulose production under co-factor regeneration conditions than the free enzyme combination. These results demonstrate that variations in the concentration of metals and synthesis conditions of nanoflowers can be extended to efficiently immobilize recombinant his-tagged enzymes. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ROYAL SOC CHEMISTRY | - |
dc.subject | L-ARABINITOL DEHYDROGENASE | - |
dc.subject | METAL-ORGANIC FRAMEWORKS | - |
dc.subject | SYNTHETIC GAS-MIXTURE | - |
dc.subject | RARE SUGAR PRODUCTION | - |
dc.subject | METHANOL PRODUCTION | - |
dc.subject | CATALYTIC-ACTIVITY | - |
dc.subject | FACILE SYNTHESIS | - |
dc.subject | NADH OXIDASE | - |
dc.subject | NANOFLOWERS | - |
dc.subject | STABILITY | - |
dc.title | Protein-inorganic hybrid system for efficient his-tagged enzymes immobilization and its application in L-xylulose production | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kang, Yun Chan | - |
dc.identifier.doi | 10.1039/c6ra24404a | - |
dc.identifier.scopusid | 2-s2.0-85009382039 | - |
dc.identifier.wosid | 000393749200056 | - |
dc.identifier.bibliographicCitation | RSC ADVANCES, v.7, no.6, pp.3488 - 3494 | - |
dc.relation.isPartOf | RSC ADVANCES | - |
dc.citation.title | RSC ADVANCES | - |
dc.citation.volume | 7 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 3488 | - |
dc.citation.endPage | 3494 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.subject.keywordPlus | L-ARABINITOL DEHYDROGENASE | - |
dc.subject.keywordPlus | METAL-ORGANIC FRAMEWORKS | - |
dc.subject.keywordPlus | SYNTHETIC GAS-MIXTURE | - |
dc.subject.keywordPlus | RARE SUGAR PRODUCTION | - |
dc.subject.keywordPlus | METHANOL PRODUCTION | - |
dc.subject.keywordPlus | CATALYTIC-ACTIVITY | - |
dc.subject.keywordPlus | FACILE SYNTHESIS | - |
dc.subject.keywordPlus | NADH OXIDASE | - |
dc.subject.keywordPlus | NANOFLOWERS | - |
dc.subject.keywordPlus | STABILITY | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.