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

Discovery of an acidic, thermostable and highly NADP+ dependent formate dehydrogenase from... Biotechnol Lett (2018) 40:1135–1147 https://doi.org/10.1007/s10529-018-2568-6 ORIGINAL RESEARCH PAPER Discovery of an acidic, thermostable and highly NADP dependent formate dehydrogenase from Lactobacillus buchneri NRRL B-30929 . . . . ˘ ¨ Saadet Alpdagtas¸ Sevil Yucel Handan Ac¸elya Kapkac¸ Siqing Liu Barıs¸ Binay Received: 15 March 2018 / Accepted: 15 May 2018 / Published online: 18 May 2018 Springer Science+Business Media B.V., part of Springer Nature 2018 Abstract protein obtained as a single band of approx. 44 kDa on Objectives To identify a robust NADP dependent SDS-PAGE and 90 kDa on native-PAGE. The formate dehydrogenase from Lactobacillus buchneri LbFDH was highly active at acidic conditions (pH NRRL B-30929 (LbFDH) with unique biochemical 4.8–6.2). Its optimum temperature was 60 C and ? ? properties. 50 C with NADP and NAD , respectively and its Results A new NADP dependent formate dehydro- T value was 78 C. Its activity did not decrease after genase gene (fdh) was cloned from genomic DNA of incubation in a solution containing 20% of DMSO and L. buchneri NRRL B-30929. The recombinant con- acetonitrile for 6 h. The K constants were 49.8, 0.12 ? ? struct was expressed in Escherichia coli BL21(DE3) and 1.68 mM for formate (with http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology Letters Springer Journals

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

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Publisher
Springer Journals
Copyright
Copyright © 2018 by Springer Science+Business Media B.V., part of Springer Nature
Subject
Life Sciences; Microbiology; Biotechnology; Applied Microbiology; Biochemistry, general
ISSN
0141-5492
eISSN
1573-6776
D.O.I.
10.1007/s10529-018-2568-6
Publisher site
See Article on Publisher Site

Abstract

Biotechnol Lett (2018) 40:1135–1147 https://doi.org/10.1007/s10529-018-2568-6 ORIGINAL RESEARCH PAPER Discovery of an acidic, thermostable and highly NADP dependent formate dehydrogenase from Lactobacillus buchneri NRRL B-30929 . . . . ˘ ¨ Saadet Alpdagtas¸ Sevil Yucel Handan Ac¸elya Kapkac¸ Siqing Liu Barıs¸ Binay Received: 15 March 2018 / Accepted: 15 May 2018 / Published online: 18 May 2018 Springer Science+Business Media B.V., part of Springer Nature 2018 Abstract protein obtained as a single band of approx. 44 kDa on Objectives To identify a robust NADP dependent SDS-PAGE and 90 kDa on native-PAGE. The formate dehydrogenase from Lactobacillus buchneri LbFDH was highly active at acidic conditions (pH NRRL B-30929 (LbFDH) with unique biochemical 4.8–6.2). Its optimum temperature was 60 C and ? ? properties. 50 C with NADP and NAD , respectively and its Results A new NADP dependent formate dehydro- T value was 78 C. Its activity did not decrease after genase gene (fdh) was cloned from genomic DNA of incubation in a solution containing 20% of DMSO and L. buchneri NRRL B-30929. The recombinant con- acetonitrile for 6 h. The K constants were 49.8, 0.12 ? ? struct was expressed in Escherichia coli BL21(DE3) and 1.68 mM for formate (with

Journal

Biotechnology LettersSpringer Journals

Published: May 18, 2018

References

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