دورية أكاديمية
Novel NAD-independent D-lactate dehydrogenases from Acetobacter aceti and Acidocella species MX-AZ02 as potential candidates for in vitro biocatalytic pyruvate production
| العنوان: | Novel NAD-independent D-lactate dehydrogenases from Acetobacter aceti and Acidocella species MX-AZ02 as potential candidates for in vitro biocatalytic pyruvate production |
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| المؤلفون: | Min, Kyoungseon, Yeon, Young Joo, Um, Youngsoon, Kim, Yong Hwan |
| بيانات النشر: | ELSEVIER SCIENCE SA |
| سنة النشر: | 2016 |
| المجموعة: | ScholarWorks@UNIST (Ulsan National Institute of Science and Technology) |
| مصطلحات موضوعية: | Bioconversion lactic acid, Biotransformations, Enzyme biocatalysis, NAD-independent d-lactate dehydrogenase, Pyruvate production |
| الوصف: | 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. ; close |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1369-703X |
| العلاقة: | BIOCHEMICAL ENGINEERING JOURNAL, v.105, no., pp.358 - 363; http://www.sciencedirect.com/science/article/pii/S1369703X15300784Test; https://scholarworks.unist.ac.kr/handle/201301/20322Test; 3192; 26718; 2-s2.0-84945151424; 000367776500005 |
| DOI: | 10.1016/j.bej.2015.10.008 |
| الإتاحة: | https://doi.org/10.1016/j.bej.2015.10.008Test https://scholarworks.unist.ac.kr/handle/201301/20322Test http://www.sciencedirect.com/science/article/pii/S1369703X15300784Test |
| رقم الانضمام: | edsbas.D9131192 |
| قاعدة البيانات: | BASE |
| تدمد: | 1369703X |
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| DOI: | 10.1016/j.bej.2015.10.008 |