Affiliation:
1. Key Laboratory of Bioorganic Synthesis of Zhejiang Province College of Biotechnology and Bioengineering Zhejiang University of Technology Hangzhou PR China
2. Engineering Research Center of Bioconversion and Biopurification of Ministry of Education Zhejiang University of Technology Hangzhou PR China
3. National and Local Joint Engineering Research Center for Biomanufacturing of Chiral Chemicals Zhejiang University of Technology Hangzhou PR China
Abstract
AbstractEnzymatic synthesis of β‐nicotinamide mononucleotide (NMN) from D‐ribose has garnered widespread attention due to its cheap material, the use of mild reaction conditions, and the ability to produce highly pure products with the desired optical properties. However, the overall NMN yield of this method is impeded by the low activity of rate‐limiting enzymes. The ribose‐phosphate diphosphokinase (PRS) and nicotinamide phosphoribosyltransferase (NAMPT), that control the rate of the reaction, were engineered to improve the reaction efficacy. The actives of mutants PRS‐H150Q and NAMPT‐Y15S were 334% and 57% higher than that of their corresponding wild‐type enzymes, respectively. Furthermore, by adding pyrophosphatase, the byproduct pyrophosphate which can inhibit the activity of NAMPT was degraded, leading to a 6.72% increase in NMN yield. Following with reaction‐process reinforcement, a high yield of 8.10 g L−1 NMN was obtained after 3 h of reaction, which was 56.86‐fold higher than that of the stepwise reaction synthesis (0.14 g L−1), indicating that the in vitro enzymatic synthesis of NMN from D‐ribose and niacinamide is an economical and feasible route.
Funder
National Key Research and Development Program of China
Cited by
4 articles.
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