Efficient Production of 2-Deoxyribose 5-Phosphate from Glucose and Acetaldehyde by Coupling of the Alcoholic Fermentation System of Baker’s Yeast and Deoxyriboaldolase-ExpressingEscherichia coli
Autor: | Mie Sasaki, Yoichi Mikami, Jun Ogawa, Nobuyuki Horinouchi, Takafumi Sakai, Takako Kawano, Seiichiro Matsumoto, Sakayu Shimizu, Kyota Saito |
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Rok vydání: | 2006 |
Předmět: |
Deoxyribose-phosphate aldolase
Acetaldehyde Saccharomyces cerevisiae Ethanol fermentation Applied Microbiology and Biotechnology Biochemistry Phosphates Analytical Chemistry chemistry.chemical_compound Potassium phosphate Escherichia coli Fructosediphosphates Molecular Biology Aldehyde-Lyases Chromatography Molecular Structure Organic Chemistry Temperature Fructose General Medicine Phosphate Yeast Klebsiella pneumoniae Glucose chemistry Alcohols Fermentation Ribosemonophosphates Biotechnology |
Zdroj: | Bioscience, Biotechnology, and Biochemistry. 70:1371-1378 |
ISSN: | 1347-6947 0916-8451 |
DOI: | 10.1271/bbb.50648 |
Popis: | 2-Deoxyribose 5-phosphate production through coupling of the alcoholic fermentation system of baker's yeast and deoxyriboaldolase-expressing Escherichia coli was investigated. In this process, baker's yeast generates fructose 1,6-diphosphate from glucose and inorganic phosphate, and then the E. coli convert the fructose 1,6-diphosphate into 2-deoxyribose 5-phosphate via D-glyceraldehyde 3-phosphate. Under the optimized conditions with toluene-treated yeast cells, 356 mM (121 g/l) fructose 1,6-diphosphate was produced from 1,111 mM glucose and 750 mM potassium phosphate buffer (pH 6.4) with a catalytic amount of AMP, and the reaction supernatant containing the fructose 1,6-diphosphate was used directly as substrate for 2-deoxyribose 5-phosphate production with the E. coli cells. With 178 mM enzymatically prepared fructose 1,6-diphosphate and 400 mM acetaldehyde as substrates, 246 mM (52.6 g/l) 2-deoxyribose 5-phosphate was produced. The molar yield of 2-deoxyribose 5-phosphate as to glucose through the total two step reaction was 22.1%. The 2-deoxyribose 5-phosphate produced was converted to 2-deoxyribose with a molar yield of 85% through endogenous or exogenous phosphatase activity. |
Databáze: | OpenAIRE |
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