Discovery of an acidic, thermostable and highly NADP+ dependent formate dehydrogenase from Lactobacillus buchneri NRRL B-30929

Biotechnology Letters
Saadet AlpdağtaşBarış Binay

Abstract

To identify a robust NADP+ dependent formate dehydrogenase from Lactobacillus buchneri NRRL B-30929 (LbFDH) with unique biochemical properties. A new NADP+ dependent formate dehydrogenase gene (fdh) was cloned from genomic DNA of L. buchneri NRRL B-30929. The recombinant construct was expressed in Escherichia coli BL21(DE3) with 6 × histidine at the C-terminus and the purified protein obtained as a single band of approx. 44 kDa on SDS-PAGE and 90 kDa on native-PAGE. The LbFDH was highly active at acidic conditions (pH 4.8-6.2). Its optimum temperature was 60 °C and 50 °C with NADP+ and NAD+, respectively and its Tm value was 78 °C. Its activity did not decrease after incubation in a solution containing 20% of DMSO and acetonitrile for 6 h. The KM constants were 49.8, 0.12 and 1.68 mM for formate (with NADP+), NADP+ and NAD+, respectively. An NADP+ dependent FDH from L. buchneri NRRL B-30929 was cloned, expressed and identified with its unusual characteristics. The LbFDH can be a promising candidate for NADPH regeneration through biocatalysis requiring acidic conditions and high temperatures.

References

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Citations

Jun 12, 2019·The Journal of Biological Chemistry·Juthamas JaroensukPimchai Chaiyen
Oct 16, 2018·Chemical Science·Simone Morra, Anca Pordea
Oct 3, 2020·Journal of Biotechnology·Cheng-Hao CaoYu-Guo Zheng
Nov 7, 2020·World Journal of Microbiology & Biotechnology·Siqing LiuNasib Qureshi
Aug 1, 2020·ACS Catalysis·Liliana Calzadiaz-RamirezCarlos G Acevedo-Rocha
Oct 12, 2021·Critical Reviews in Biotechnology·Saadet AlpdağtaşBarış Binay

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Datasets Mentioned

BETA
EAY67119.1
ACF35003.1
AEU36496.1
AIY34662.1

Methods Mentioned

BETA
PCR
column chromatography
electrophoresis
Differential scanning calorimetry

Software Mentioned

COBALT
- Hit Initiated BLAST ( PHIBLAST )
Origin
PHIBLAST search
Pattern
BioEdit

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