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DC Field | Value | Language |
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dc.citation.endPage | 138 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 131 | - |
dc.citation.title | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | - |
dc.citation.volume | 15 | - |
dc.contributor.author | Raj, Subramanian Mohan | - |
dc.contributor.author | Rathnasingh, Chelladurai | - |
dc.contributor.author | Jung, Woo-Chel | - |
dc.contributor.author | Selvakumar, Edwardraja | - |
dc.contributor.author | Park, Sunghoon | - |
dc.date.accessioned | 2023-12-22T07:14:55Z | - |
dc.date.available | 2023-12-22T07:14:55Z | - |
dc.date.created | 2017-02-19 | - |
dc.date.issued | 2010-01 | - |
dc.description.abstract | 3-Hydroxypropionic acid (3-HP), a versatile and valuable platform chemical, has diverse industrial applications; but its biological production from glycerol is often limited by the capability of the enzyme aldehyde dehydrogenase (ALDH) to convert an intermediary compound, 3-hydroxypropionaldehyde (3-HPA), to 3-HP. In this study, we report a new ALDH, PuuC, from Klebsiella pneumoniae DSM 2026, that efficiently converts 3-HPA to 3-HP. The identified gene puuC was cloned, expressed in Escherichia coli, purified, and characterized for its properties. The recombinant enzyme with a molecular weight of 53.8 kDa exhibited broad substrate specificity for various aliphatic aldehydes, especially C-2-C-5 aldehydes. NAD(+) was the preferred coenzyme for the oxidation of most aliphatic and aromatic aldehydes tested. The optimum pH and temperature for PuuC activity were pH 8.0 and 45 degrees C. The K-m values for 3-HPA and NAD(+) were 0.48 and 0.09 mM, respectively. The activity of PuuC was enhanced in the presence of reducing agents such as 2-mercaptoethanol or dithiothreitol, while several metal ions, particularly Hg2+, Ag+, and Cu2+ inhibited its activity. The predicted structure of PuuC indicated the presence of K191 and E194 in close proximity to the glycine motif, suggesting that PuuC belongs to class 2 ALDHs. | - |
dc.identifier.bibliographicCitation | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.15, no.1, pp.131 - 138 | - |
dc.identifier.doi | 10.1007/s12257-010-0030-2 | - |
dc.identifier.issn | 1226-8372 | - |
dc.identifier.scopusid | 2-s2.0-77953558759 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/25347 | - |
dc.identifier.url | https://link.springer.com/article/10.1007%2Fs12257-010-0030-2 | - |
dc.identifier.wosid | 000275163800016 | - |
dc.language | 영어 | - |
dc.publisher | KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING | - |
dc.title | A Novel NAD(+)-dependent Aldehyde Dehydrogenase Encoded by the puuC Gene of Klebsiella pneumoniae DSM 2026 that Utilizes 3-Hydroxypropionaldehyde as a Substrate | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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