Improved stability and reusability of endoglucanase from Clostridium thermocellum by a biosilica-based auto-encapsulation method
DC Field | Value | Language |
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dc.contributor.author | Ryu, Young Ha | - |
dc.contributor.author | Yeo, Ki Baek | - |
dc.contributor.author | Ki, Mi-Ran | - |
dc.contributor.author | Kim, Yong Jun | - |
dc.contributor.author | Pack, Seung Pil | - |
dc.date.accessioned | 2021-09-04T03:49:45Z | - |
dc.date.available | 2021-09-04T03:49:45Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2016-01-15 | - |
dc.identifier.issn | 1369-703X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/89786 | - |
dc.description.abstract | The functional improvement of endoglucanase (EG), a key cellulose-hydrolyzing biocatalyst, is imperative for the practical use of cellulosic materials such as lignocellulose, stove and straws. Here, we employed a bio-inspired silica-encapsulation method to improve the stability and reusability of EG. We introduced a new silica-forming peptide (SFP) from Ectocarpus siliculosus at the C-terminus of EG to generate a recombinant fusion protein, EG-SFP, with auto-silicifying ability. We obtained an EG-SFP-encapsulated silica matrix (EG-SFP@Silica) via the EG-SFP-mediated auto-silicification process under ambient conditions. The immobilization efficiency was 90%. The introduction of SFP did not significantly affect the functionality of EG, and moreover, EG-SFP@Silica demonstrated higher thermostability by 5 degrees C than free EG-SFP or EG. In addition, EG-SFP@Silica retained 90% of its initial residual activity with up to 18 uses. These results provide a platform for the development of a practical enzymatic hydrolysis process for cellulosic materials. (C) 2015 Elsevier B.V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | ENZYME IMMOBILIZATION | - |
dc.subject | SILICA | - |
dc.subject | PROTEIN | - |
dc.title | Improved stability and reusability of endoglucanase from Clostridium thermocellum by a biosilica-based auto-encapsulation method | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Ki, Mi-Ran | - |
dc.contributor.affiliatedAuthor | Kim, Yong Jun | - |
dc.contributor.affiliatedAuthor | Pack, Seung Pil | - |
dc.identifier.doi | 10.1016/j.bej.2015.09.006 | - |
dc.identifier.scopusid | 2-s2.0-84942531836 | - |
dc.identifier.wosid | 000367776300016 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL ENGINEERING JOURNAL, v.105, pp.144 - 149 | - |
dc.relation.isPartOf | BIOCHEMICAL ENGINEERING JOURNAL | - |
dc.citation.title | BIOCHEMICAL ENGINEERING JOURNAL | - |
dc.citation.volume | 105 | - |
dc.citation.startPage | 144 | - |
dc.citation.endPage | 149 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Engineering | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Engineering, Chemical | - |
dc.subject.keywordPlus | ENZYME IMMOBILIZATION | - |
dc.subject.keywordPlus | SILICA | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordAuthor | Cellulase | - |
dc.subject.keywordAuthor | Immobilised enzymes | - |
dc.subject.keywordAuthor | Immobilization | - |
dc.subject.keywordAuthor | Polypeptides | - |
dc.subject.keywordAuthor | Biosilicification | - |
dc.subject.keywordAuthor | Silica forming peptide | - |
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