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DC Field | Value | Language |
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dc.citation.endPage | 363 | - |
dc.citation.startPage | 358 | - |
dc.citation.title | BIOCHEMICAL ENGINEERING JOURNAL | - |
dc.citation.volume | 105 | - |
dc.contributor.author | Min, Kyoungseon | - |
dc.contributor.author | Yeon, Young Joo | - |
dc.contributor.author | Um, Youngsoon | - |
dc.contributor.author | Kim, Yong Hwan | - |
dc.date.accessioned | 2023-12-22T00:12:52Z | - |
dc.date.available | 2023-12-22T00:12:52Z | - |
dc.date.created | 2016-09-06 | - |
dc.date.issued | 2016-01 | - |
dc.description.abstract | Pyruvate is a significant platform chemical widely used in the agrochemical and pharmaceutical industries. We discovered FAD-containing lactate dehydrogenases (LDHs) from Acetobacter aceti (Aa-LDH) and Acidocella species MX-AZ02 (As-LDH), expressed them in Escherichia coil, optimized their FAD reconstitution, and characterized the recombinants as NAD-independent D-LDHs that are capable of the in vitro biocatalytic production of pyruvate from lactate. Instead of NAD, both Aa-LDH and As-LDH utilized various organic dyes as the electron acceptor. In addition, Aa-LDH and As-LDH exhibited substrate specificity for D-lactate only. Activity was optimized at pH 7.0 and 65 degrees C. The kinetic parameters of Aa-LDH and As-LDH were examined and both enzymes exhibited higher catalytic efficiency (k(cat)/K-m) for 2,6-dichlorophenolindophenol (DCIP), one of the electron acceptors, than D-lactate due to higher binding affinities. When using 10 mM D-lactate as the substrate with stepwise DCIP and D-LDH feeding, Aa-LDH and As-LDH produced 5.48 and 4.09 mM pyruvate, respectively, and the conversion was proportional to the DCIP concentration. | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL ENGINEERING JOURNAL, v.105, pp.358 - 363 | - |
dc.identifier.doi | 10.1016/j.bej.2015.10.008 | - |
dc.identifier.issn | 1369-703X | - |
dc.identifier.scopusid | 2-s2.0-84945151424 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/20322 | - |
dc.identifier.url | http://www.sciencedirect.com/science/article/pii/S1369703X15300784 | - |
dc.identifier.wosid | 000367776500005 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCIENCE SA | - |
dc.title | Novel NAD-independent D-lactate dehydrogenases from Acetobacter aceti and Acidocella species MX-AZ02 as potential candidates for in vitro biocatalytic pyruvate production | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | Enzyme biocatalysis | - |
dc.subject.keywordAuthor | Bioconversion lactic acid | - |
dc.subject.keywordAuthor | Biotransformations | - |
dc.subject.keywordAuthor | NAD-independent D-lactate dehydrogenase | - |
dc.subject.keywordAuthor | Pyruvate production | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | ACID | - |
dc.subject.keywordPlus | STRAIN | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | CELLS | - |
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