Creating a new benzaldehyde lyase for atom-economic synthesis of chiral 1,2,4-butanetriol and 2-aminobutane-1,4-diol from formaldehyde

Liu, Yu; Yao, Peng-Fei; Zhang, Shiqing; Feng, Jinhui; Sheng, Hao; Liu, Xiangtao; Sheng, Xiang; Wu, Qingping; Zhu, Dunming; Ma, Yanhe

doi:10.1016/j.checat.2022.11.006

Cited by 11 publications

(8 citation statements)

References 67 publications

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“…Formaldehyde is an emerging C1 resource since it can be easily derived from carbon monoxide, carbon dioxide, formic acid, methane, and methanol by biological or chemical means (Desmons et al 2019 ; Jo et al 2022 ). Formaldehyde-converting enzymes such as formolase, benzaldehyde lyase, and pyruvate aldolase are the key biocatalysts in the synthesis of value-added chemicals from C1 feedstocks (Güner et al 2021 ; Hernandez et al 2017 ; Li et al 2023 ; Siegel et al 2015 ). Despite considerable research on this subject, the progress achieved so far has not translated into highly efficient catalyst systems or processes that enable large-scale industrial application.…”

Section: Introductionmentioning

confidence: 99%

Biotransformation of 2-keto-4-hydroxybutyrate via aldol condensation using an efficient and thermostable carboligase from Deinococcus radiodurans

Jeong,

Seo,

Sung

et al. 2024

Bioresour. Bioprocess.

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The bioconversion of 4-hydroxy-2-keto acid derivatives via aldol condensation of formaldehyde and pyruvate has received substantial attention as potential source of chemicals for production of amino acids, hydroxy carboxylic acids, and chiral aldehydes. We developed an environmentally friendly biocatalyst consisting of a novel thermostable class II pyruvate aldolase from Deinococcus radiodurans with maltose-binding protein (MBP-DrADL), which has specific activity of 46.3 µmol min–1 mg–1. Surprisingly, MBP-DrADL maintained over 60% of enzyme activity for 4 days at 50 to 65 °C, we used MBP-DrADL as the best candidate enzyme to produce 2-keto-4-hydroxybutyrate (2-KHB) from formaldehyde and pyruvate via aldol condensation. The optimum reaction conditions for 2-KHB production were 50 °C, pH 8.0, 5 mM Mg2+, 100 mM formaldehyde, and 200 mM pyruvate. Under these optimized conditions, MBP-DrADL produced 76.5 mM (8.94 g L–1) 2-KHB over 60 min with a volumetric productivity of 8.94 g L–1 h–1 and a specific productivity of 357.6 mg mg-enzyme–1 h–1. Furthermore, 2-KHB production was improved by continuous addition of substrates, which produced approximately 124.8 mM (14.6 g L–1) of 2-KHB over 60 min with a volumetric productivity and specific productivity of 14.6 g L–1 h–1 and 583.4 mg mg-enzyme–1 h–1, respectively. MBP-DrADL showed the highest specific productivity for 2-KHB production yet reported. Our study provides a highly efficient biocatalyst for the synthesis of 2-KHB and lays the foundation for large-scale production and application of high-value compounds from formaldehyde. Graphical Abstract

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Section: Introductionmentioning

confidence: 99%

Biotransformation of 2-keto-4-hydroxybutyrate via aldol condensation using an efficient and thermostable carboligase from Deinococcus radiodurans

Jeong,

Seo,

Sung

et al. 2024

Bioresour. Bioprocess.

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“…1,2,4-Butanetriol (1,2,4-BT) is a platform chemical with versatile applications [ 9 ]. The most important application of 1,2,4-BT is to produce 1,2,4-butanetriol trinitrate (BTTN).…”

Section: Introductionmentioning

confidence: 99%

Efficient production of 1,2,4-butanetriol from corn cob hydrolysate by metabolically engineered Escherichia coli

Li,

Wang,

et al. 2024

Microb Cell Fact

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Corn cob is a major waste mass-produced in corn agriculture. Corn cob hydrolysate containing xylose, arabinose, and glucose is the hydrolysis product of corn cob. Herein, a recombinant Escherichia coli strain BT-10 was constructed to transform corn cob hydrolysate into 1,2,4-butanetriol, a platform substance with diversified applications. To eliminate catabolite repression and enhance NADPH supply for alcohol dehydrogenase YqhD catalyzed 1,2,4-butanetriol generation, ptsG encoding glucose transporter EIICBGlc and pgi encoding phosphoglucose isomerase were deleted. With four heterologous enzymes including xylose dehydrogenase, xylonolactonase, xylonate dehydratase, α-ketoacid decarboxylase and endogenous YqhD, E. coli BT-10 can produce 36.63 g/L 1,2,4-butanetriol with a productivity of 1.14 g/[L·h] using xylose as substrate. When corn cob hydrolysate was used as the substrate, 43.4 g/L 1,2,4-butanetriol was generated with a productivity of 1.09 g/[L·h] and a yield of 0.9 mol/mol. With its desirable characteristics, E. coli BT-10 is a promising strain for commercial 1,2,4-butanetriol production.

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“…Thiamine diphosphate (ThDP)-dependent enzymes catalyze C–C bond ligation and cleavage reactions, including pyruvate decarboxylase (PDC), benzoylformate decarboxylase (BFD), benzaldehyde lyase (BAL), transketolase (TK), and so on. − In the previous studies, the α-hydroxymethyl ketones have been prepared by direct hydroxymethylation of aldehydes with formaldehyde using BAL and other enzymes through C–C bond formation. ,,,,− However, it has been observed that the homocoupling of aldehyde is competing with the hydroxymethylation to give the acyloin byproduct in the BAL-catalyzed reactions. Cosolvents such as 2-methyltetrahydrofuran and large excess of formaldehyde have been used to reduce the homocoupling product, but the reaction still must be carried out at low substrate concentration. , Zhang et al reported that 1-(furan-2-yl)-2-hydroxyethan-1-one could be obtained from furfural (50 g/L) and formaldehyde through increasing the solubility of PDC from Sulfobacillus sp.…”

Section: Introductionmentioning

confidence: 99%

Manipulating Activity and Chemoselectivity of a Benzaldehyde Lyase for Efficient Synthesis of α-Hydroxymethyl Ketones and One-Pot Enantio-Complementary Conversion to 1,2-Diols

Zhang,

Li,

Chen

et al. 2024

ACS Catal.

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Creating a new benzaldehyde lyase for atom-economic synthesis of chiral 1,2,4-butanetriol and 2-aminobutane-1,4-diol from formaldehyde

Cited by 11 publications

References 67 publications

Biotransformation of 2-keto-4-hydroxybutyrate via aldol condensation using an efficient and thermostable carboligase from Deinococcus radiodurans

Biotransformation of 2-keto-4-hydroxybutyrate via aldol condensation using an efficient and thermostable carboligase from Deinococcus radiodurans

Efficient production of 1,2,4-butanetriol from corn cob hydrolysate by metabolically engineered Escherichia coli

Manipulating Activity and Chemoselectivity of a Benzaldehyde Lyase for Efficient Synthesis of α-Hydroxymethyl Ketones and One-Pot Enantio-Complementary Conversion to 1,2-Diols

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