Efficient production of inositol from glucose via a tri-enzymatic cascade pathway

Wang, Jiaping; Cheng, Hui; Zhao, Zhihong; Zhang, Yimin

doi:10.1016/j.biortech.2022.127125

“…Assembling enzymes in one-pot, and especially in one cell, should solve the crucial problem of unbalanced enzyme activity ratios. This problem can be addressed using enzyme expression regulation strategies, such as promoter replacement, [22] RBS regulation, [23] multi-plasmid systems, [17] gene copies modification, [24] and protein engineering. [25] The efficient production of target compounds from inexpensive building block molecules can be obtained after optimizing reaction conditions.…”

Section: Introductionmentioning

confidence: 99%

Efficient Production of L‐Homophenylalanine by Enzymatic‐Chemical Cascade Catalysis

Gao

¹

,

Song

²

,

Wu

³

et al. 2022

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L-Homophenylalanine (L-HPA) is a vital building block for the synthesis of numerous chiral drugs. However, the high cost of starting materials limits the industrial production of L-HPA. In this study, an enzymatic-spontaneous chemical cascade route for L-HPA production was designed based on retrosynthetic analysis. This route, using simple benzaldehyde and pyruvate as starting materials, is extremely cost-effective. The enzymes were screened and further assembled in E. coli, and TipheDH was identified as the ratelimiting enzyme. Therefore, TipheDH was engineered to improve its specific activity (by 82 %) and expression level (by 254 %), thus generating the best strain (W14). W14 exhibited the optimum enzyme activity ratio (1.7 : 1.1 : 1 : 1.8) and demonstrated production of 100.9 g L À 1 of L-HPA (with 94 % conversion, > 99 % ee) in a 5-L reactor. This route effectively exploits the power of cascades and offers insight into avenues for synthesizing other valuable chemicals from inexpensive building blocks.

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Efficient Production of L‐Homophenylalanine by Enzymatic‐Chemical Cascade Catalysis

Gao

¹

,

Song

²

,

Wu

³

et al. 2022

View full text Add to dashboard Cite

L-Homophenylalanine (L-HPA) is a vital building block for the synthesis of numerous chiral drugs. However, the high cost of starting materials limits the industrial production of L-HPA. In this study, an enzymatic-spontaneous chemical cascade route for L-HPA production was designed based on retrosynthetic analysis. This route, using simple benzaldehyde and pyruvate as starting materials, is extremely cost-effective. The enzymes were screened and further assembled in E. coli, and TipheDH was identified as the ratelimiting enzyme. Therefore, TipheDH was engineered to improve its specific activity (by 82 %) and expression level (by 254 %), thus generating the best strain (W14). W14 exhibited the optimum enzyme activity ratio (1.7 : 1.1 : 1 : 1.8) and demonstrated production of 100.9 g L À 1 of L-HPA (with 94 % conversion, > 99 % ee) in a 5-L reactor. This route effectively exploits the power of cascades and offers insight into avenues for synthesizing other valuable chemicals from inexpensive building blocks.

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Transcriptome sequencing reveals key metabolic pathways for the synthesis of L-serine from glycerol and glucose in Escherichia coli

Chen

¹

,

Li

²

,

Zhou

³

et al. 2023

Biochemical Engineering Journal

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Efficient production of inositol from glucose via a tri-enzymatic cascade pathway

Cited by 8 publications

References 42 publications

Efficient Production of L‐Homophenylalanine by Enzymatic‐Chemical Cascade Catalysis

Efficient Production of L‐Homophenylalanine by Enzymatic‐Chemical Cascade Catalysis

Efficient Production of L‐Homophenylalanine by Enzymatic‐Chemical Cascade Catalysis

Transcriptome sequencing reveals key metabolic pathways for the synthesis of L-serine from glycerol and glucose in Escherichia coli

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