Enhancement of l-valine production in Bacillus licheniformis by blocking three branched pathways

Liang, Chong; Huo, Yanli; Qi, Gaofu; Wei, Xuetuan; Wang, Qin; Chen, Shouwen

doi:10.1007/s10529-015-1783-7

Cited by 14 publications

(5 citation statements)

References 15 publications

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“…The efficient application of the valine has been advanced by engineered Corynebacterium glutamicum [ 166 ], E . coli [ 167 ], Bacillus subtilis [ 168 ], Bacillus licheniformis [ 169 ], Saccharomyces cerevisiae [ 165 ]. In animal nutrition, the appropriate L -valine produced by fermentation using E .…”

Section: Discussionmentioning

confidence: 99%

The biological functions and metabolic pathways of valine in swine

Wang,

Peng,

Zhang

et al. 2023

J Animal Sci Biotechnol

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Valine is an essential amino acid and a type of branched-chain amino acid. Due to the involvement of branched-chain amino acids in various metabolic pathways, there has been a surge of interests in valine nutrition and its role in animal physiology. In pigs, the interactions between valine and other branched-chain amino acids or aromatic amino acids are complex. In this review, we delve into the interaction mechanism, metabolic pathways, and biological functions of valine. Appropriate valine supplementation not only enhances growth and reproductive performances, but also modulates gut microbiota and immune functions. Based on past observations and interpretations, we provide recommended feed levels of valine for weaned piglets, growing pigs, gilts, lactating sows, barrows and entire males. The summarized valine nutrient requirements for pigs at different stages offer valuable insights for future research and practical applications in animal husbandry.

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Section: Discussionmentioning

confidence: 99%

The biological functions and metabolic pathways of valine in swine

Wang,

Peng,

Zhang

et al. 2023

J Animal Sci Biotechnol

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“…The fused fragment (1140 bp) was digested with Xba I and Sac I, and inserted into T2(2)-ori, generating plasmid T2Δ gdh . Transformation of B. licheniformis WX-02 with the knock-out plasmid T2Δ gdh was performed via electroporation based on the previous protocols [ 33 ]. The kanamycin-resistant transformants were picked and verified by PCR with the primers T2-VF and T2-VR.…”

Section: Methodsmentioning

confidence: 99%

Engineering Bacillus licheniformis for the production of meso-2,3-butanediol

Qiu

Zhang

et al. 2016

Biotechnol Biofuels

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Background2,3-Butanediol (2,3-BD) can be used as a liquid fuel additive to replace petroleum oil, and as an important platform chemical in the pharmaceutical and plastic industries. Microbial production of 2,3-BD by Bacillus licheniformis presents potential advantages due to its GRAS status, but previous attempts to use this microorganism as a chassis strain resulted in the production of a mix of D-2,3-BD and meso-2,3-BD isomers.ResultsThe aim of this work was to develop an engineered strain of B. licheniformis suited to produce the high titers of the pure meso-2,3-BD isomer. Glycerol dehydrogenase (Gdh) was identified as the catalyst for D-2,3-BD biosynthesis from its precursor acetoin in B. licheniformis. The gdh gene was, therefore, deleted from the wild-type strain WX-02 to inhibit the flux of acetoin to D-2,3-BD biosynthesis. The acoR gene involved in acetoin degradation through AoDH ES was also deleted to provide adequate flux from acetoin towards meso-2,3-BD. By re-directing the carbon flux distribution, the double-deletion mutant WX-02ΔgdhΔacoR produced 28.2 g/L of meso-2,3-BD isomer with >99 % purity. The titer was 50 % higher than that of the wide type. A bench-scale fermentation by the double-deletion mutant was developed to further improve meso-2,3-BD production. In a fed-batch fermentation, meso-2,3-BD titer reached 98.0 g/L with a purity of >99.0 % and a productivity of 0.94 g/L–h.ConclusionsThis work demonstrates the potential of producing meso-2,3-BD with high titer and purity through metabolic engineering of B. licheniformis.Electronic supplementary materialThe online version of this article (doi:10.1186/s13068-016-0522-1) contains supplementary material, which is available to authorized users.

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“…In addition, with the individual disruption of leu or ilvA in Bacillus licheniformis WX-02, L-Val production increased by 22 and 14 times with a titer of 33.2 and 21.1 mmol/L, respectively. Further disruption of ldh in WX-02 ∆leuA improved L-Val productivity to 0.47 mmol/L per hour [ 147 ].…”

Section: L-valinementioning

confidence: 99%

Recent Advances in Metabolic Engineering for the Biosynthesis of Phosphoenol Pyruvate–Oxaloacetate–Pyruvate-Derived Amino Acids

Yin,

Zhou,

Ding

et al. 2024

Molecules

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The phosphoenol pyruvate–oxaloacetate–pyruvate-derived amino acids (POP-AAs) comprise native intermediates in cellular metabolism, within which the phosphoenol pyruvate–oxaloacetate–pyruvate (POP) node is the switch point among the major metabolic pathways existing in most living organisms. POP-AAs have widespread applications in the nutrition, food, and pharmaceutical industries. These amino acids have been predominantly produced in Escherichia coli and Corynebacterium glutamicum through microbial fermentation. With the rapid increase in market requirements, along with the global food shortage situation, the industrial production capacity of these two bacteria has encountered two bottlenecks: low product conversion efficiency and high cost of raw materials. Aiming to push forward the update and upgrade of engineered strains with higher yield and productivity, this paper presents a comprehensive summarization of the fundamental strategy of metabolic engineering techniques around phosphoenol pyruvate–oxaloacetate–pyruvate node for POP-AA production, including L-tryptophan, L-tyrosine, L-phenylalanine, L-valine, L-lysine, L-threonine, and L-isoleucine. Novel heterologous routes and regulation methods regarding the carbon flux redistribution in the POP node and the formation of amino acids should be taken into consideration to improve POP-AA production to approach maximum theoretical values. Furthermore, an outlook for future strategies of low-cost feedstock and energy utilization for developing amino acid overproducers is proposed.

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Enhancement of l-valine production in Bacillus licheniformis by blocking three branched pathways

Abstract: We provide a possibility to over-produce L-valine using genetically-modified B. licheniformis using remodeling of the biosynthetic pathway to L-valine.

Cited by 14 publications

References 15 publications

The biological functions and metabolic pathways of valine in swine

The biological functions and metabolic pathways of valine in swine

Engineering Bacillus licheniformis for the production of meso-2,3-butanediol

Recent Advances in Metabolic Engineering for the Biosynthesis of Phosphoenol Pyruvate–Oxaloacetate–Pyruvate-Derived Amino Acids

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