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DC Field | Value | Language |
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dc.citation.endPage | 979 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 971 | - |
dc.citation.title | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | - |
dc.citation.volume | 20 | - |
dc.contributor.author | Lama, Suman | - |
dc.contributor.author | Ro, Su Moon | - |
dc.contributor.author | Seol, Eunhee | - |
dc.contributor.author | Sekar, Balaji Sundara | - |
dc.contributor.author | Ainala, Satish Kumar | - |
dc.contributor.author | Thangappan, Jayaraman | - |
dc.contributor.author | Song, Hyohak | - |
dc.contributor.author | Seung, Doyoung | - |
dc.contributor.author | Park, Sunghoon | - |
dc.date.accessioned | 2023-12-22T00:36:51Z | - |
dc.date.available | 2023-12-22T00:36:51Z | - |
dc.date.created | 2017-02-19 | - |
dc.date.issued | 2015-11 | - |
dc.description.abstract | 1,3-propanediol oxidoreductase (DhaT) of Klebsiella pneumoniae converts 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol (1,3-PD) during microbial production of 1,3-PD from glycerol. In this study, DhaT from newly isolated K. pneumoniae J2B was cloned, expressed, purified, and studied for its kinetic properties. It showed, on its physiological substrate 3-HPA, higher activity than similar aldehydes such as acetaldehyde, propionaldehyde and butyraldehyde. The turnover numbers (k (cat) , 1/s) were estimated as 59.4 for the forward reaction (3-HPA to 1,3-PD at pH 7.0) and 10.0 for the reverse reaction (1,3-PD to 3-HPA at pH 9.0). The Michaelis constants (K (m) , mM) were 0.77 (for 3-HPA) and 0.03 (for NADH) for the forward reaction (at pH 7.0), and 7.44 (for 1,3-PD) and 0.23 (for NAD(+)) for the reverse reaction (at pH 9.0). Between these forward and reverse reactions, the optimum temperature and pH were significantly different (37A degrees C and 7.0 vs. 55A degrees C and 9.0, respectively). These results indicate that, under physiological conditions, DhaT mostly catalyzes the forward reaction. The enzyme was seriously inhibited by heavy metal ions such as Ag+ and Hg2+. DhaT was highly unstable when incubated with its own substrate 3-HPA, indicating the necessity of enhancing its stability for improved 1,3-PD production from glycerol. | - |
dc.identifier.bibliographicCitation | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.20, no.6, pp.971 - 979 | - |
dc.identifier.doi | 10.1007/s12257-015-0635-6 | - |
dc.identifier.issn | 1226-8372 | - |
dc.identifier.scopusid | 2-s2.0-84954493454 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/25305 | - |
dc.identifier.url | http://link.springer.com/article/10.1007%2Fs12257-015-0635-6 | - |
dc.identifier.wosid | 000368366700001 | - |
dc.language | 영어 | - |
dc.publisher | KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING | - |
dc.title | Characterization of 1,3-propanediol oxidoreductase (DhaT) from Klebsiella pneumoniae J2B | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | 1,3-propanediol oxidoreductase | - |
dc.subject.keywordAuthor | 3-hydroxy-propionaldehyde | - |
dc.subject.keywordAuthor | 1,3-propanediol | - |
dc.subject.keywordAuthor | Klebsiella pneumoniae | - |
dc.subject.keywordPlus | ENTEROBACTER-AGGLOMERANS | - |
dc.subject.keywordPlus | CITROBACTER-FREUNDII | - |
dc.subject.keywordPlus | MICROBIAL-PRODUCTION | - |
dc.subject.keywordPlus | DEHYDROGENASE | - |
dc.subject.keywordPlus | 3-HYDROXYPROPIONALDEHYDE | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | GLYCEROL | - |
dc.subject.keywordPlus | ACCUMULATION | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | CLONING | - |
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