Enhancing β-alanine production from glucose in genetically modified Corynebacterium glutamicum by metabolic pathway engineering

Wang, Jinyu; Rao, Zhiming; Xu, Jianzhong; Zhang, Weiguo

doi:10.1007/s00253-021-11696-y

Cited by 19 publications

(12 citation statements)

References 36 publications

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“…Lys, as an inhibitor, could inhibit AK activity and decrease the affinity for Asp, which was consistent with data shown in Fig. 3 and previous literature [ 15 ]. The Kd value for T379L/A380M-Lys + Asp was 373.79 mM, indicating that the affinity between the mutant and the substrate Asp (373.79 mM) was greater than that with WT-AK (701.25 mM) in the presence of Lys.…”

Section: Resultssupporting

confidence: 93%

Characterization of aspartokinase double mutants using a combination of experiments and simulations

Chen

Liu

et al. 2023

Heliyon

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Section: Resultssupporting

confidence: 93%

Characterization of aspartokinase double mutants using a combination of experiments and simulations

Chen

Liu

et al. 2023

Heliyon

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“…In prokaryotes, beta-alanine is mainly produced by decarboxylation of L-aspartate by L-aspartate 1-decarboxylase ( Cronan, 1980 ) ( Figure 1 ). Extensive metabolic engineering of Escherichia coli and Corynebacterium glutamicum has already resulted in strains producing 85 g/L and 56 g/L beta-alanine from glucose, respectively ( Wang et al, 2021 ; Li et al, 2022 ).…”

Section: Introductionmentioning

confidence: 99%

Production of biopolymer precursors beta-alanine and L-lactic acid from CO2 with metabolically versatile Rhodococcus opacus DSM 43205

Salusjärvi

Ojala²,

Peddinti³

et al. 2022

Front. Bioeng. Biotechnol.

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Hydrogen oxidizing autotrophic bacteria are promising hosts for conversion of CO2 into chemicals. In this work, we engineered the metabolically versatile lithoautotrophic bacterium R. opacus strain DSM 43205 for synthesis of polymer precursors. Aspartate decarboxylase (panD) or lactate dehydrogenase (ldh) were expressed for beta-alanine or L-lactic acid production, respectively. The heterotrophic cultivations on glucose produced 25 mg L−1 beta-alanine and 742 mg L−1 L-lactic acid, while autotrophic cultivations with CO2, H2, and O2 resulted in the production of 1.8 mg L−1 beta-alanine and 146 mg L−1 L-lactic acid. Beta-alanine was also produced at 345 μg L−1 from CO2 in electrobioreactors, where H2 and O2 were provided by water electrolysis. This work demonstrates that R. opacus DSM 43205 can be engineered to produce chemicals from CO2 and provides a base for its further metabolic engineering.

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“…ADCs from bacteria including Bacillus subtilis , Escherichia coli and Corynebacterium glutamicum have been well studied and used for β-alanine synthesis in the laboratory [ 9 , 12 , 20 , 25 ]. For example, by expressing ADC from C. glutamicum in E. coli for whole-cell catalysis, β-alanine production reached 24.8 g/L with a yield of 92.6% after 20 h of reaction [ 25 ].…”

Section: Introductionmentioning

confidence: 99%

MpADC, an l-aspartate-α-decarboxylase, from Myzus persicae, that enables production of β-alanine with high yield by whole-cell enzymatic catalysis

Liu,

Xie,

Guo

et al. 2023

Biotechnol Biofuels

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Background β-Alanine is a precursor of many important pharmaceutical products and food additives, its market demand is continuously increasing nowadays. Whole-cell catalysis relying on the recombinant expression of key β-alanine synthesizing enzymes is an important method to produce β-alanine. Nevertheless, β-alanine synthesizing enzymes found so far have problems including easy inactivation, low expression or poor catalytic activity, and it remains necessary to develop new enzymes. Results Herein, we characterized an l-aspartate-α-decarboxylase, MpADC, from an aphid, Myzus persicae. It showed excellent catalytic activity at pH 6.0–7.5 and 37 °C. With the help of chaperone co-expression and N-terminal engineering guided by AlphaFold2 structure prediction, the expression and catalytic ability of MpADC in Escherichia coli were significantly improved. Using 50 g/L of E. coli cells expressing the MpADC-∆39 variant cultured in a 15-L fermenter, 232.36 g/L of β-alanine was synthesized in 13.5 h, with the average β-alanine yield of 17.22 g/L/h, which is best known so far. Conclusions Our research should facilitate the production of β-alanine in an environment-friendly manner.

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Enhancing β-alanine production from glucose in genetically modified Corynebacterium glutamicum by metabolic pathway engineering

Cited by 19 publications

References 36 publications

Characterization of aspartokinase double mutants using a combination of experiments and simulations

Characterization of aspartokinase double mutants using a combination of experiments and simulations

Production of biopolymer precursors beta-alanine and L-lactic acid from CO2 with metabolically versatile Rhodococcus opacus DSM 43205

MpADC, an l-aspartate-α-decarboxylase, from Myzus persicae, that enables production of β-alanine with high yield by whole-cell enzymatic catalysis

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