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김용환

Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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Novel NAD-independent D-lactate dehydrogenases from Acetobacter aceti and Acidocella species MX-AZ02 as potential candidates for in vitro biocatalytic pyruvate production

Author(s)
Min, KyoungseonYeon, Young JooUm, YoungsoonKim, Yong Hwan
Issued Date
2016-01
DOI
10.1016/j.bej.2015.10.008
URI
https://scholarworks.unist.ac.kr/handle/201301/20322
Fulltext
http://www.sciencedirect.com/science/article/pii/S1369703X15300784
Citation
BIOCHEMICAL ENGINEERING JOURNAL, v.105, pp.358 - 363
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.
Publisher
ELSEVIER SCIENCE SA
ISSN
1369-703X
Keyword (Author)
Enzyme biocatalysisBioconversion lactic acidBiotransformationsNAD-independent D-lactate dehydrogenasePyruvate production
Keyword
ESCHERICHIA-COLIACIDSTRAINPURIFICATIONENZYMECELLS

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