Detailed Information

Cited 0 time in webofscience Cited 0 time in scopus
Metadata Downloads

Improved stability and reusability of endoglucanase from Clostridium thermocellum by a biosilica-based auto-encapsulation method

Full metadata record
DC Field Value Language
dc.contributor.authorRyu, Young Ha-
dc.contributor.authorYeo, Ki Baek-
dc.contributor.authorKi, Mi-Ran-
dc.contributor.authorKim, Yong Jun-
dc.contributor.authorPack, Seung Pil-
dc.date.accessioned2021-09-04T03:49:45Z-
dc.date.available2021-09-04T03:49:45Z-
dc.date.created2021-06-18-
dc.date.issued2016-01-15-
dc.identifier.issn1369-703X-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/89786-
dc.description.abstractThe 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.languageEnglish-
dc.language.isoen-
dc.publisherELSEVIER SCIENCE BV-
dc.subjectENZYME IMMOBILIZATION-
dc.subjectSILICA-
dc.subjectPROTEIN-
dc.titleImproved stability and reusability of endoglucanase from Clostridium thermocellum by a biosilica-based auto-encapsulation method-
dc.typeArticle-
dc.contributor.affiliatedAuthorKi, Mi-Ran-
dc.contributor.affiliatedAuthorKim, Yong Jun-
dc.contributor.affiliatedAuthorPack, Seung Pil-
dc.identifier.doi10.1016/j.bej.2015.09.006-
dc.identifier.scopusid2-s2.0-84942531836-
dc.identifier.wosid000367776300016-
dc.identifier.bibliographicCitationBIOCHEMICAL ENGINEERING JOURNAL, v.105, pp.144 - 149-
dc.relation.isPartOfBIOCHEMICAL ENGINEERING JOURNAL-
dc.citation.titleBIOCHEMICAL ENGINEERING JOURNAL-
dc.citation.volume105-
dc.citation.startPage144-
dc.citation.endPage149-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiotechnology & Applied Microbiology-
dc.relation.journalResearchAreaEngineering-
dc.relation.journalWebOfScienceCategoryBiotechnology & Applied Microbiology-
dc.relation.journalWebOfScienceCategoryEngineering, Chemical-
dc.subject.keywordPlusENZYME IMMOBILIZATION-
dc.subject.keywordPlusSILICA-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordAuthorCellulase-
dc.subject.keywordAuthorImmobilised enzymes-
dc.subject.keywordAuthorImmobilization-
dc.subject.keywordAuthorPolypeptides-
dc.subject.keywordAuthorBiosilicification-
dc.subject.keywordAuthorSilica forming peptide-
Files in This Item
There are no files associated with this item.
Appears in
Collections
Graduate School > Department of Food and Biotechnology > 1. Journal Articles
Graduate School > Department of Biotechnology and Bioinformatics > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher Kim, Young Jun photo

Kim, Young Jun
Department of Food and Biotechnology
Read more

Altmetrics

Total Views & Downloads

BROWSE