There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 488 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 477 | - |
dc.citation.title | JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY | - |
dc.citation.volume | 44 | - |
dc.contributor.author | Sankaranarayanan, Mugesh | - |
dc.contributor.author | Seol, Eunhee | - |
dc.contributor.author | Kim, Yeonhee | - |
dc.contributor.author | Chauhan, Ashish Singh | - |
dc.contributor.author | Park, Sunghoon | - |
dc.date.accessioned | 2023-12-21T22:37:24Z | - |
dc.date.available | 2023-12-21T22:37:24Z | - |
dc.date.created | 2017-06-14 | - |
dc.date.issued | 2017-03 | - |
dc.description.abstract | Glycerol dehydratase (GDHt), which converts glycerol to 3-hydroxypropionaldehyde, is essential to the production of 1,3-propanediol (1,3-PDO) or 3-hydroxypropionic acid (3-HP). A reliable GDHt activity assay in crude-cell extract was developed. In the assay, GDHt converted 1,2-propanediol (1,2-PDO) to propionaldehyde, which was further converted to 1-propionic acid by aldehyde dehydrogenase (KGSADH) or to 1-propanol by yeast-alcohol dehydrogenase (yADH), while the NADH concentration change was monitored spectrophotometrically. Cells should be disintegrated by Bead Beater/French Press, not by chemical methods (BugBuster (R)/B-PER (TM)), because the reagents significantly inactivated GDHt and coupling enzymes. Furthermore, in the assay mixture, a much higher activity of KGSADH (> 200-fold) or yADH (> 400-fold) than that of GDHt should have been maintained. Under optimal conditions, both KGSADH and yADH showed practically the same activity. The coupled-enzyme assay method established here should prove to be applicable to recombinant strains developed for the production of 3-HP and/or 1,3-PDO from glycerol. | - |
dc.identifier.bibliographicCitation | JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY, v.44, no.3, pp.477 - 488 | - |
dc.identifier.doi | 10.1007/s10295-017-1902-7 | - |
dc.identifier.issn | 1367-5435 | - |
dc.identifier.scopusid | 2-s2.0-85009485697 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/22217 | - |
dc.identifier.url | https://link.springer.com/article/10.1007%2Fs10295-017-1902-7 | - |
dc.identifier.wosid | 000395204400015 | - |
dc.language | 영어 | - |
dc.publisher | SPRINGER HEIDELBERG | - |
dc.title | Measurement of crude-cell-extract glycerol dehydratase activity in recombinant Escherichia coli using coupled-enzyme reactions | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.