ArticleScientific reports2019
Optimization of a reduced enzymatic reaction cascade for the production of L-alanine.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Extending Cofactor-Tethered Nanomachines to Complex Multienzyme Redox Cascades in Continuous Flow.ChemSusChem · 2026Article
- De Novo Biosynthesis of Valinomycin From Glucose Using In Vitro Reconstituted Hybrid Pathways.Chembiochem : a European journal of chemical biology · 2026Article
- Plug-and-play - enzymatic amino acid production from methanol and carbon dioxide.Nature communications · 2026Article
- Article
- Tartrate Dehydrogenase in Bacillus Species: Deciphering Unique Catalytic Diversity Through Kinetic, Structural and Molecular Docking Analysis.The protein journal · 2024Article
- Efficient biosynthesis of D/L-alanine in the recombinantFrontiers in bioengineering and biotechnology · 2024Article
- Lactic Acid from COEnvironmental science & technology · 2023Article
- Structure-Guided Modulation of the Catalytic Properties of [2Fe-2S]-Dependent Dehydratases.Chembiochem : a European journal of chemical biology · 2022Article
- Directed evolution of alditol oxidase for the production of optically pure D-glycerate from glycerol in the engineered Escherichia coli.Journal of industrial microbiology & biotechnology · 2021Article
- Development of an Improved Peroxidase-Based High-Throughput Screening for the Optimization of D-Glycerate Dehydratase Activity.International journal of molecular sciences · 2020Article
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3 authors.
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Abstract
Cell-free enzymatic reaction cascades combine the advantages of well-established in vitro biocatalysis with the power of multi-step in vivo pathways. The absence of a regulatory cell environment enables direct process control including methods for facile bottleneck identification and process optimization. Within this work, we developed a reduced, enzymatic reaction cascade for the direct production of L-alanine from D-glucose and ammonium sulfate. An efficient, activity based enzyme selection is demonstrated for the two branches of the cascade. The resulting redox neutral cascade is composed of a glucose dehydrogenase, two dihydroxyacid dehydratases, a keto-deoxy-aldolase, an aldehyde dehydrogenase and an L-alanine dehydrogenase. This artificial combination of purified biocatalysts eliminates the need for phosphorylation and only requires NAD as cofactor. We provide insight into in detail optimization of the process parameters applying a fluorescamine based L-alanine quantification assay. An optimized enzyme ratio and the necessary enzyme load were identified and together with the optimal concentrations of cofactor (NAD), ammonium and buffer yields of >95% for the main branch and of 8% for the side branch were achieved.
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