β-Alanine production by L-aspartate-α-decarboxylase from Corynebacterium glutamicum and variants with reduced substrate inhibition

Wang, Jing; Ma, Ding; Mai, Dandan; Li, Huanhuan; Wang, Jingwen; Wang, Xin; Chen, Kequan; Ouyang, Pingkai

doi:10.1016/j.mcat.2022.112246

Cited by 3 publications

(2 citation statements)

References 26 publications

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“…L-aspartate-α-decarboxylase (EC 4.1.1.11,ADC) catalyzes the synthesis of β-alanine from L-aspartate (Piao et al, 2019;Wang et al, 2022; (Figure 8). Compared to nitrilases, ADCs have a high substrate concentration and a high conversion rate, so the synthesis of β-alanine is more productive, and at the end of the reaction, the reaction system has a low concentration of byproducts and substrate, which greatly reduces the cost of purification.…”

Section: L-aspartate As Substratementioning

confidence: 99%

“…It is possible to increase the self-cleavage efficiency of ADCs by mutation of these sites, thereby increasing the active protein content and enhancing enzyme activity. Increasing the tolerated substrate concentration, which can increase the yield and reduce wastewater discharge, is an important factor for industrial applications, and the tolerated substrate concentration was dramatically increased by the C. glutamicum ADC R12V and Q17A mutations (Wang et al, 2022).…”

Section: Fumaric Acid As Substratementioning

confidence: 99%

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Advances in the synthesis of β-alanine

Song,

Zhang,

Wang

et al. 2023

Front. Bioeng. Biotechnol.

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β-Alanine is the only naturally occurring β-type amino acid in nature, and it is also one of the very promising three-carbon platform compounds that can be applied in cosmetics and food additives and as a precursor in the chemical, pharmaceutical and material fields, with very broad market prospects. β-Alanine can be synthesized through chemical and biological methods. The chemical synthesis method is relatively well developed, but the reaction conditions are extreme, requiring high temperature and pressure and strongly acidic and alkaline conditions; moreover, there are many byproducts that require high energy consumption. Biological methods have the advantages of product specificity, mild conditions, and simple processes, making them more promising production methods for β-alanine. This paper provides a systematic review of the chemical and biological synthesis pathways, synthesis mechanisms, key synthetic enzymes and factors influencing β-alanine, with a view to providing a reference for the development of a highly efficient and green production process for β-alanine and its industrialization, as well as providing a basis for further innovations in the synthesis of β-alanine.

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Section: L-aspartate As Substratementioning

confidence: 99%

Section: Fumaric Acid As Substratementioning

confidence: 99%

Advances in the synthesis of β-alanine

Song,

Zhang,

Wang

et al. 2023

Front. Bioeng. Biotechnol.

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Fine and combinatorial regulation of key metabolic pathway for enhanced β‐alanine biosynthesis with non‐inducible Escherichia coli

Zhou,

Ding,

Zhang

et al. 2024

Biotech & Bioengineering

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Abstractβ‐Alanine is the only β‐amino acid in nature and one of the most important three‐carbon chemicals. This work was aimed to construct a non‐inducible β‐alanine producer with enhanced metabolic flux towards β‐alanine biosynthesis in Escherichia coli. First of all, the assembled E. coli endogenous promoters and 5′‐untranslated regions (PUTR) were screened to finely regulate the combinatorial expression of genes panDBS and aspBCG for an optimal flux match between two key pathways. Subsequently, additional copies of key genes (panDBSK104S and ppc) were chromosomally introduced into the host A1. On these bases, dynamical regulation of the gene thrA was performed to reduce the carbon flux directed in the competitive pathway. Finally, the β‐alanine titer reached 10.25 g/L by strain A14‐R15, 361.7% higher than that of the original strain. Under fed‐batch fermentation in a 5‐L fermentor, a titer of 57.13 g/L β‐alanine was achieved at 80 h. This is the highest titer of β‐alanine production ever reported using non‐inducible engineered E. coli. This metabolic modification strategy for optimal carbon flux distribution developed in this work could also be used for the production of various metabolic products.

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One-Pot Synthesis of β-Alanine from Fumaric Acid via an Efficient Dual-Enzyme Cascade Biotransformation

Ni,

Zhang,

Nie

et al. 2024

Biomolecules

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As the only naturally occurring β-amino acid, β-alanine has important application prospects in many fields. Driven by the huge demand, biosynthesis is becoming more and more popular as a potential alternative to the chemical synthesis of β-alanine. Although the direct pathway from L-aspartic acid to β-alanine, catalyzed by L-aspartic acid-α-decarboxylase (PanD), is ideal for β-alanine synthesis, it is hindered by the high cost of the substrate and limited economic viability. In this work, a cell-free dual enzyme cascade system based on methylaspartate lyase (EcMAL) and panD was constructed to safely and efficiently synthesize β-alanine using fumarate as a substrate. Taking the previously engineered EcMAL as the target, CgPanD was finally screened as the best candidate through gene mining, sequence alignment, and enzyme property analysis. Finally, under the optimal conditions of 35 °C, pH 8.0, and EcMAL: CgPanD concentration ratio of 1:5, the yield of β-alanine reached 80% theoretical yield within 120 min. This study provides a potential strategy for the biosynthesis of β-alanine, paving the way for future industrial-scale production.

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β-Alanine production by L-aspartate-α-decarboxylase from Corynebacterium glutamicum and variants with reduced substrate inhibition

Cited by 3 publications

References 26 publications

Advances in the synthesis of β-alanine

Advances in the synthesis of β-alanine

Fine and combinatorial regulation of key metabolic pathway for enhanced β‐alanine biosynthesis with non‐inducible Escherichia coli

One-Pot Synthesis of β-Alanine from Fumaric Acid via an Efficient Dual-Enzyme Cascade Biotransformation

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