Improving Biosynthesis Efficiency of Nicotinamide Mononucleotide by ATP Recycling Engineering and Condition Optimization DOI
Cun‐Duo Tang,

T. C. Shen,

Xueyang Bai

et al.

Journal of Agricultural and Food Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: April 23, 2025

Nicotinamide mononucleotide (NMN) is a very important bioactive nucleotide that of great help to human health. However, its widespread application has been limited by high production costs, especially the cost core substrates, coenzyme, and enzymes. In this study, ADP/GDP-polyphosphate phosphotransferase RhPPK2 originating from Rhodobacter sphaeroides was successfully expressed in Escherichia coli with high-level solubility, enzyme activity lysate supernatant reached 21.9 ± 0.65 U/mL. And then, temperature profiles, pH kinetic parameters purified reRhPPK2 were systematically characterized, which demonstrate potential for enzymatic ATP regeneration systems. Furthermore, introduction significantly enhanced NMN efficiency, achieving 2.3-fold increase compared conventional supplementation method. Finally, efficiency further improved single-factor experiment L9(34) orthogonal design, yield up 14.6 0.51 g/L, about 5.4 times initial yield. This research substantially reduced costs established robust foundation industrial-scale production.

Language: Английский

Improving Biosynthesis Efficiency of Nicotinamide Mononucleotide by ATP Recycling Engineering and Condition Optimization DOI
Cun‐Duo Tang,

T. C. Shen,

Xueyang Bai

et al.

Journal of Agricultural and Food Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: April 23, 2025

Nicotinamide mononucleotide (NMN) is a very important bioactive nucleotide that of great help to human health. However, its widespread application has been limited by high production costs, especially the cost core substrates, coenzyme, and enzymes. In this study, ADP/GDP-polyphosphate phosphotransferase RhPPK2 originating from Rhodobacter sphaeroides was successfully expressed in Escherichia coli with high-level solubility, enzyme activity lysate supernatant reached 21.9 ± 0.65 U/mL. And then, temperature profiles, pH kinetic parameters purified reRhPPK2 were systematically characterized, which demonstrate potential for enzymatic ATP regeneration systems. Furthermore, introduction significantly enhanced NMN efficiency, achieving 2.3-fold increase compared conventional supplementation method. Finally, efficiency further improved single-factor experiment L9(34) orthogonal design, yield up 14.6 0.51 g/L, about 5.4 times initial yield. This research substantially reduced costs established robust foundation industrial-scale production.

Language: Английский

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