Heterologous expression of Deinococcus geothermalis amylosucrase in Corynebacterium glutamicum for luteolin glucoside production
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chin Y.-W. | - |
dc.contributor.author | Jang S.-W. | - |
dc.contributor.author | Shin H.-S. | - |
dc.contributor.author | Kim T.-W. | - |
dc.contributor.author | Kim S.-K. | - |
dc.contributor.author | Park C.-S. | - |
dc.contributor.author | Seo D.-H. | - |
dc.date.available | 2020-03-03T06:46:57Z | - |
dc.date.created | 2020-02-24 | - |
dc.date.issued | 2020-04 | - |
dc.identifier.issn | 0141-0229 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/17795 | - |
dc.description.abstract | Amylosucrase (ASase) has great industrial potential owing to its multifunctional activities, including transglucosylation, polymerization, and isomerization. In the present study, the properties of Deinococcus geothermalis ASase (DGAS) expressed in Corynebacterium glutamicum (cDGAS) and purified via Ni-NTA affinity chromatography were compared to those of DGAS expressed in Escherichia coli (eDGAS). The pH profile of cDGAS was similar to that of eDGAS, whereas the temperature profile of cDGAS was lower than that of eDGAS. The melting temperature of both enzymes did not differ significantly. Interestingly, polymerization activity was slightly lower in cDGAS than in eDGAS, whereas luteolin (an acceptor molecule) transglucosylation activity in cDGAS was 10 % higher than that in eDGAS. Analysis of protein secondary structure via circular dichroism spectroscopy revealed that cDGAS had a lower strand/helix ratio than eDGAS. The present results indicate that cDGAS is of greater industrial significance than eDGAS. © 2019 Elsevier Inc. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | Elsevier Inc. | - |
dc.relation.isPartOf | Enzyme and Microbial Technology | - |
dc.title | Heterologous expression of Deinococcus geothermalis amylosucrase in Corynebacterium glutamicum for luteolin glucoside production | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000521513900010 | - |
dc.identifier.doi | 10.1016/j.enzmictec.2019.109505 | - |
dc.identifier.bibliographicCitation | Enzyme and Microbial Technology, v.135 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.scopusid | 2-s2.0-85077322427 | - |
dc.citation.title | Enzyme and Microbial Technology | - |
dc.citation.volume | 135 | - |
dc.contributor.affiliatedAuthor | Jang S.-W. | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | Amylosucrases | - |
dc.subject.keywordAuthor | Corynebacterium glutamicum | - |
dc.subject.keywordAuthor | Deinococcus geothermalis | - |
dc.subject.keywordAuthor | Heterologous expression | - |
dc.subject.keywordAuthor | Luteolin | - |
dc.subject.keywordAuthor | Transglucosylation | - |
dc.subject.keywordPlus | Affinity chromatography | - |
dc.subject.keywordPlus | Dichroism | - |
dc.subject.keywordPlus | Escherichia coli | - |
dc.subject.keywordPlus | Flavonoids | - |
dc.subject.keywordPlus | Polymerization | - |
dc.subject.keywordPlus | Amylosucrases | - |
dc.subject.keywordPlus | Corynebacterium glutamicum | - |
dc.subject.keywordPlus | Deinococcus geothermalis | - |
dc.subject.keywordPlus | Heterologous expression | - |
dc.subject.keywordPlus | Luteolin | - |
dc.subject.keywordPlus | Transglucosylation | - |
dc.subject.keywordPlus | Circular dichroism spectroscopy | - |
dc.subject.keywordPlus | amylosucrase | - |
dc.subject.keywordPlus | luteolin | - |
dc.subject.keywordPlus | sucrase | - |
dc.subject.keywordPlus | unclassified drug | - |
dc.subject.keywordPlus | affinity chromatography | - |
dc.subject.keywordPlus | anion exchange chromatography | - |
dc.subject.keywordPlus | Article | - |
dc.subject.keywordPlus | circular dichroism | - |
dc.subject.keywordPlus | controlled study | - |
dc.subject.keywordPlus | Corynebacterium glutamicum | - |
dc.subject.keywordPlus | Deinococcus | - |
dc.subject.keywordPlus | Deinococcus geothermalis | - |
dc.subject.keywordPlus | enzyme activity | - |
dc.subject.keywordPlus | enzyme purification | - |
dc.subject.keywordPlus | Escherichia coli | - |
dc.subject.keywordPlus | heterologous expression | - |
dc.subject.keywordPlus | high performance liquid chromatography | - |
dc.subject.keywordPlus | melting temperature | - |
dc.subject.keywordPlus | nonhuman | - |
dc.subject.keywordPlus | polymerization | - |
dc.subject.keywordPlus | protein secondary structure | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
1342, Seongnam-daero, Sujeong-gu, Seongnam-si, Gyeonggi-do, Republic of Korea(13120)031-750-5114
COPYRIGHT 2020 Gachon 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.