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Discovery and characterization of a thermostable d-lactate dehydrogenase from Lactobacillus jensenii through genome mining

Paper ID Volume ID Publish Year Pages File Format Full-Text
34854 45052 2013 9 PDF Available
Title
Discovery and characterization of a thermostable d-lactate dehydrogenase from Lactobacillus jensenii through genome mining
Abstract

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 °C) than the others. The T5010 value of this thermostable d-LDH3 was 48.3 °C, much higher than the T5010 values of the others (42.7 and 42.9 °C) and that of a commercial d-lactate dehydrogenase (41.2 °C). The Tm values were 48.6, 45.7 and 55.7 °C for the three d-LDHs, respectively. In addition, kinetic parameter (kcat/Km) 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 °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.

► Three kinds of d-lactate dehydrogenase from genome of Lactobacillus jensenii were expressed in E. coli. ► d-LDH3 exhibited higher optimal temperature up to 50 °C compared with those of other d-LDHs. ► The catalytic efficiency (kcat/Km) of d-LDH3 for pyruvate conversion was estimated to be 200 times higher than that for lactate conversion at pH 8.0 and 25 °C. ► The d-LDH3 can be a good candidate biocatalyst for the d-lactate production at high temperature.

Keywords
d-Lactate dehydrogenase; d-Lactic acid; Lactobacillus jensenii; Thermostability
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Discovery and characterization of a thermostable d-lactate dehydrogenase from Lactobacillus jensenii through genome mining
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 48, Issue 1, January 2013, Pages 109–117
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us