Discovery of an acidic, thermostable and highly NADP(+) dependent formate dehydrogenase from Lactobacillus buchneri NRRL B-30929
BIOTECHNOLOGY LETTERS, vol.40, pp.1135-1147, 2018 (SCI-Expanded, Scopus)
- Publication Type: Article / Article
- Volume: 40
- Publication Date: 2018
- Doi Number: 10.1007/s10529-018-2568-6
- Journal Name: BIOTECHNOLOGY LETTERS
- Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Page Numbers: pp.1135-1147
- Keywords: Acidic formate dehydrogenase, Biochemical and kinetic characterization, Highly NADP(+) dependent formate dehydrogenase, Lactobacillus buchneri NRRL B-30929, Solvent stable, Thermostability, HIGH-RESOLUTION STRUCTURES, COENZYME SPECIFICITY, COFACTOR SPECIFICITY, ENZYME
- Yıldız Technical University Affiliated: Yes
Abstract
To identify a robust NADP(+) dependent formate dehydrogenase from Lactobacillus buchneri NRRL B-30929 (LbFDH) with unique biochemical properties.