High-Performance Production of <i>N</i>-Acetyl-<scp>d</scp>-Neuraminic Acid with Whole Cells of Fast-Growing <i>Vibrio natriegens</i> via a Thermal Strategy

Peng, Yuan; Ma, Lina; Xu, Ping; Tao, Fei

doi:10.1021/acs.jafc.3c07259

Cited by 3 publications

(2 citation statements)

References 58 publications

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“…The widespread use of synthetic biology has made possible the mass production of some functional bioactive substances. Currently, the yield of glutamine can reach an impressive 73.5 g/L (Lv et al, 2021), whereas sialic acid can achieve 126.1 g/L (Peng et al, 2023) in fermented broth through the application of synthetic biology strategies. Synthetic biology, an interdisciplinary field that seamlessly combines biology and engineering, has emerged as an invaluable tool for the biosynthesis of therapeutic proteins, drugs, and other active molecules (Pardee et al, 2016).…”

Section: Application Of Synthetic Biology For a High Yield Of Glutami...mentioning

confidence: 99%

Glutamine‐derived peptides: Current progress and future directions

Yu,

Hu,

et al. 2024

Comp Rev Food Sci Food Safe

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Glutamine, the most abundant amino acid in the body, plays a critical role in preserving immune function, nitrogen balance, intestinal integrity, and resistance to infection. However, its limited solubility and instability present challenges for its use a functional nutrient. Consequently, there is a preference for utilizing glutamine‐derived peptides as an alternative to achieve enhanced functionality. This article aims to review the applications of glutamine monomers in clinical, sports, and enteral nutrition. It compares the functional effectiveness of monomers and glutamine‐derived peptides and provides a comprehensive assessment of glutamine‐derived peptides in terms of their classification, preparation, mechanism of absorption, and biological activity. Furthermore, this study explores the potential integration of artificial intelligence (AI)‐based peptidomics and synthetic biology in the de novo design and large‐scale production of these peptides. The findings reveal that glutamine‐derived peptides possess significant structure‐related bioactivities, with the smaller molecular weight fraction serving as the primary active ingredient. These peptides possess the ability to promote intestinal homeostasis, exert hypotensive and hypoglycemic effects, and display antioxidant properties. However, our understanding of the structure–function relationships of glutamine‐derived peptides remains largely exploratory at current stage. The combination of AI based peptidomics and synthetic biology presents an opportunity to explore the untapped resources of glutamine‐derived peptides as functional food ingredients. Additionally, the utilization and bioavailability of these peptides can be enhanced through the use of delivery systems in vivo. This review serves as a valuable reference for future investigations of and developments in the discovery, functional validation, and biomanufacturing of glutamine‐derived peptides in food science.

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Section: Application Of Synthetic Biology For a High Yield Of Glutami...mentioning

confidence: 99%

Glutamine‐derived peptides: Current progress and future directions

Yu,

Hu,

et al. 2024

Comp Rev Food Sci Food Safe

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“…With whole-cell catalytic mode, the accumulation of GSH had reached 7.68 g/L with an engineered E. coli strain (Cui et al, 2019), and further increased to 10.4 g/L in E. coli JM109 with the couple of S. cerevisiae cells (Li et al, 2011). While enzymatic synthesis has achieved high yields of GSH, the whole-cell catalytic synthesis of GSH shows promising potential for development with many advantages (Domach, 2015;Peng et al, 2023).…”

mentioning

confidence: 99%

Efficient production of l‐glutathione by whole‐cell catalysis with ATP regeneration from adenosine

Zuo,

Zhao,

Zhang

et al. 2024

Biotech & Bioengineering

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Abstractl‐glutathione (GSH) is an important tripeptide compound with extensive applications in medicine, food additives, and cosmetics industries. In this work, an innovative whole‐cell catalytic strategy was developed to enhance GSH production by combining metabolic engineering of GSH biosynthetic pathways with an adenosine‐based adenosine triphosphate (ATP) regeneration system in Escherichia coli. Concretely, to enhance GSH production in E. coli, several genes associated with GSH and l‐cysteine degradation, as well as the branched metabolic flow, were deleted. Additionally, the GSH bifunctional synthase (GshFSA) and GSH ATP‐binding cassette exporter (CydDC) were overexpressed. Moreover, an adenosine‐based ATP regeneration system was first introduced into E. coli to enhance GSH biosynthesis without exogenous ATP additions. Through the optimization of whole‐cell catalytic conditions, the engineered strain GSH17‐FDC achieved an impressive GSH titer of 24.19 g/L only after 2 h reaction, with a nearly 100% (98.39%) conversion rate from the added l‐Cys. This work not only unveils a new platform for GSH production but also provides valuable insights for the production of other high‐value metabolites that rely on ATP consumption.

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Economical one-pot synthesis of isoquercetin and D-allulose from quercetin and sucrose using whole-cell biocatalyst

Wang,

Zhang

et al. 2024

Enzyme and Microbial Technology

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High-Performance Production of N-Acetyl-d-Neuraminic Acid with Whole Cells of Fast-Growing Vibrio natriegens via a Thermal Strategy

Cited by 3 publications

References 58 publications

Glutamine‐derived peptides: Current progress and future directions

Glutamine‐derived peptides: Current progress and future directions

Efficient production of l‐glutathione by whole‐cell catalysis with ATP regeneration from adenosine

Economical one-pot synthesis of isoquercetin and D-allulose from quercetin and sucrose using whole-cell biocatalyst

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