دورية أكاديمية
Discovery and characterization of a thermostable D-lactate dehydrogenase from Lactobacillus jensenii through genome mining
| العنوان: | Discovery and characterization of a thermostable D-lactate dehydrogenase from Lactobacillus jensenii through genome mining |
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| المؤلفون: | Jun, Chanha, Sa, Young Seung, Gu, Sol-A, Joo, Jeong Chan, Kim, Seil, Kim, Kyung-Jin, Kim, Yong Hwan |
| بيانات النشر: | ELSEVIER SCI LTD |
| سنة النشر: | 2016 |
| المجموعة: | ScholarWorks@UNIST (Ulsan National Institute of Science and Technology) |
| مصطلحات موضوعية: | d-Lactate dehydrogenase, d-Lactic acid, Lactobacillus jensenii, Thermostability |
| الوصف: | The demand on thermostable D-lactate dehydrogenases (D-LDH) has been increased for D-lactic acid production but thermostable D-DLHs with industrially applicable activity were not much explored. To identify a thermostable D-LDH, three D-LDHs from different Lactobacillus jensenii strains were screened by genome mining and then expressed in Escherichia coli. One of the three D-LDHs (D-LDH3) exhibited higher optimal reaction temperature (50 degrees C) than the others. The T-50(10) value of this thermostable D-LDH3 was 48.3 degrees C, much higher than the T-50(10) values of the others (42.7 and 42.9 degrees C) and that of a commercial D-lactate dehydrogenase (41.2 degrees C). The T-m values were 48.6, 45.7 and 55.7 degrees C for the three D-LDHs, respectively. In addition, kinetic parameter (k(cat)/K-m) of D-LDH3 for pyruvate reduction was estimated to be almost 150 times higher than that for lactate oxidation at pH 8.0 and 25 degrees C, implying that D-lactate production from pyruvate is highly favored. These superior thermal and kinetic features would make the D-LDH3 characterized in this study a good candidate for the microbial production of D-lactate at high temperature from glucose if it is genetically introduced to lactate producing microbial. ; close |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1359-5113 |
| العلاقة: | PROCESS BIOCHEMISTRY, v.48, no.1, pp.109 - 117; http://www.sciencedirect.com/science/article/pii/S1359511312004163Test; https://scholarworks.unist.ac.kr/handle/201301/20357Test; 3192; 26753; 2-s2.0-84874112739; 000316426000014 |
| DOI: | 10.1016/j.procbio.2012.11.013 |
| الإتاحة: | https://doi.org/10.1016/j.procbio.2012.11.013Test https://scholarworks.unist.ac.kr/handle/201301/20357Test http://www.sciencedirect.com/science/article/pii/S1359511312004163Test |
| رقم الانضمام: | edsbas.E63873DA |
| قاعدة البيانات: | BASE |
| تدمد: | 13595113 |
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| DOI: | 10.1016/j.procbio.2012.11.013 |