Surface immobilization of protein via biosilification catalyzed by silicatein fused to glutathione S-transferase (GST).
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| Title: | Surface immobilization of protein via biosilification catalyzed by silicatein fused to glutathione S-transferase (GST). |
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| Authors: | Ki, Mi-Ran1, Yeo, Ki1, Pack, Seung1 spack@korea.ac.kr |
| Source: | Bioprocess & Biosystems Engineering. May2013, Vol. 36 Issue 5, p643-648. 6p. |
| Subjects: | Glutathione, Escherichia coli, Silicon, Enzymes, Fluorescent polymers |
| Abstract: | Silicatein from Suberites domuncula was known to catalyze silica deposition in vitro under near neutral pH and ambient temperature conditions. In this study, we employed GST-glutathione (GSH) interaction system to increase the production of silicatein and develop an efficient protein immobilization method. Recombinant silicatein fused with GST (GST-SIL) was produced in E. coli and the GST-SIL protein was employed on GSH-coated glass plate. GST-SIL bound surface or matrix can catalyze the formation of silica layer in the presence of tetraethyl orthosilicate as a substrate at an ambient temperature and neutral pH. During silicatein-mediated silicification, green fluorescent protein (GFP) or horseradish peroxidase (HRP) can be efficiently immobilized on the silica surface. Immobilized GFP or HRP retained their activity and were released gradually. This biocompatible silica coating technique can be employed to prepare biomolecule-immobilized surfaces or matrixes, which are useful for the development of biocatalytic, diagnostic and biosensing system, or tissue culture scaffolds. [ABSTRACT FROM AUTHOR] |
| Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Links: – Type: pdflink Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 87303818 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Surface immobilization of protein via biosilification catalyzed by silicatein fused to glutathione S-transferase (GST). – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Ki%2C+Mi-Ran%22">Ki, Mi-Ran</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Yeo%2C+Ki%22">Yeo, Ki</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Pack%2C+Seung%22">Pack, Seung</searchLink><relatesTo>1</relatesTo><i> spack@korea.ac.kr</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Bioprocess+%26+Biosystems+Engineering%22">Bioprocess & Biosystems Engineering</searchLink>. May2013, Vol. 36 Issue 5, p643-648. 6p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Glutathione%22">Glutathione</searchLink><br /><searchLink fieldCode="DE" term="%22Escherichia+coli%22">Escherichia coli</searchLink><br /><searchLink fieldCode="DE" term="%22Silicon%22">Silicon</searchLink><br /><searchLink fieldCode="DE" term="%22Enzymes%22">Enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Fluorescent+polymers%22">Fluorescent polymers</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Silicatein from Suberites domuncula was known to catalyze silica deposition in vitro under near neutral pH and ambient temperature conditions. In this study, we employed GST-glutathione (GSH) interaction system to increase the production of silicatein and develop an efficient protein immobilization method. Recombinant silicatein fused with GST (GST-SIL) was produced in E. coli and the GST-SIL protein was employed on GSH-coated glass plate. GST-SIL bound surface or matrix can catalyze the formation of silica layer in the presence of tetraethyl orthosilicate as a substrate at an ambient temperature and neutral pH. During silicatein-mediated silicification, green fluorescent protein (GFP) or horseradish peroxidase (HRP) can be efficiently immobilized on the silica surface. Immobilized GFP or HRP retained their activity and were released gradually. This biocompatible silica coating technique can be employed to prepare biomolecule-immobilized surfaces or matrixes, which are useful for the development of biocatalytic, diagnostic and biosensing system, or tissue culture scaffolds. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1007/s00449-012-0818-x Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 6 StartPage: 643 Subjects: – SubjectFull: Glutathione Type: general – SubjectFull: Escherichia coli Type: general – SubjectFull: Silicon Type: general – SubjectFull: Enzymes Type: general – SubjectFull: Fluorescent polymers Type: general Titles: – TitleFull: Surface immobilization of protein via biosilification catalyzed by silicatein fused to glutathione S-transferase (GST). Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Ki, Mi-Ran – PersonEntity: Name: NameFull: Yeo, Ki – PersonEntity: Name: NameFull: Pack, Seung IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 05 Text: May2013 Type: published Y: 2013 Identifiers: – Type: issn-print Value: 16157591 Numbering: – Type: volume Value: 36 – Type: issue Value: 5 Titles: – TitleFull: Bioprocess & Biosystems Engineering Type: main |
| ResultId | 1 |