Biokatalyse: Enzymatische Synthese für industrielle Anwendungen

Wu, Shuke; Šnajdrová, Radka; Moore, Jeffrey C.; Baldenius, Kai; Bornscheuer, Uwe T.

doi:10.1002/ange.202006648

Cited by 109 publications

(33 citation statements)

References 379 publications

(376 reference statements)

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“…Biotransformation is a green and sustainable approach for the production of valuable chemicals, pharmaceuticals, and materials, among others (Bornscheuer et al, 2012;Sheldon and Woodley, 2018;Wu and Li, 2018;Wang et al, 2021;Wu et al, 2021). For decades, microbial organisms have been predominantly engineered to synthesize those compounds of interest from cost-effective carbon sources like renewable biomass (e.g., cellulose and starch, etc.)…”

Section: Introductionmentioning

confidence: 99%

Designing Modular Cell-free Systems for Tunable Biotransformation of l-phenylalanine to Aromatic Compounds

Yang

Liu

et al. 2021

Front. Bioeng. Biotechnol.

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Cell-free systems have been used to synthesize chemicals by reconstitution of in vitro expressed enzymes. However, coexpression of multiple enzymes to reconstitute long enzymatic pathways is often problematic due to resource limitation/competition (e.g., energy) in the one-pot cell-free reactions. To address this limitation, here we aim to design a modular, cell-free platform to construct long biosynthetic pathways for tunable synthesis of value-added aromatic compounds, using (S)-1-phenyl-1,2-ethanediol ((S)-PED) and 2-phenylethanol (2-PE) as models. Initially, all enzymes involved in the biosynthetic pathways were individually expressed by an E. coli-based cell-free protein synthesis (CFPS) system and their catalytic activities were confirmed. Then, three sets of enzymes were coexpressed in three cell-free modules and each with the ability to complete a partial pathway. Finally, the full biosynthetic pathways were reconstituted by mixing two related modules to synthesize (S)-PED and 2-PE, respectively. After optimization, the final conversion rates for (S)-PED and 2-PE reached 100 and 82.5%, respectively, based on the starting substrate of l-phenylalanine. We anticipate that the modular cell-free approach will make a possible efficient and high-yielding biosynthesis of value-added chemicals.

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Section: Introductionmentioning

confidence: 99%

Designing Modular Cell-free Systems for Tunable Biotransformation of l-phenylalanine to Aromatic Compounds

Yang

Liu

et al. 2021

Front. Bioeng. Biotechnol.

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“…Biocatalysis has emerged as a powerful strategy to efficiently perform synthetic reactions under mild conditions, also at industrial scales. [1][2][3] In a nutshell, biocatalysis exploits nature's ability to perform chemical reactions with extraordinary selectivity and rates at ambient temperatures and pressures.…”

Section: Introductionmentioning

confidence: 99%

Applied biocatalysis beyond just buffers – from aqueous to unconventional media. Options and guidelines

Schie

Spöring

Bocola³

et al. 2021

Green Chem.

105

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“…Since LmrR_pAF is an artificial enzyme that is biosynthesized in living cells, we surmised that the catalysed hydrazone formation reaction could also be carried out in vivo. Moreover, since a variety of enzymatic synthesis of aldehydes from carboxylic acid or alcohol precursors are known, [32][33][34] we envisioned an in vivo biocatalytic cascade comprising the biosynthesis of aldehydes using canonical enzymes followed by the LmrR_V15pAF_RMH catalyzed new-to-nature hydrazone formation reaction.…”

Section: Introductionmentioning

confidence: 99%

An In Vivo Biocatalytic Cascade Featuring an Artificial Enzyme Catalyzed New-to-Nature Reaction

Atta

Zhou

Roelfes

2021

Preprint

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Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalanine (pAF) as catalytic residue are able to react with carbonyl compounds through an iminium ion mechanism, making reactions possible that have no equivalent in nature. Here, we report an in vivo biocatalytic cascade that is augmented with such an artificial enzyme catalyzed new-to-nature reaction. The artificial enzyme in this study is a pAF containing evolved variant of the Lactococcal multidrug resistance Regulator, designated LmrR_V15pAF_RMH, which efficiently converts in vivo produced benzaldehyde derivatives into the corresponding hydrazone products inside E. coli cells. These in vivo biocatalytic cascades comprising an artificial enzyme catalyzed reactions are an important step towards achieving a hybrid metabolism.

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Biokatalyse: Enzymatische Synthese für industrielle Anwendungen

Cited by 109 publications

References 379 publications

Designing Modular Cell-free Systems for Tunable Biotransformation of l-phenylalanine to Aromatic Compounds

Designing Modular Cell-free Systems for Tunable Biotransformation of l-phenylalanine to Aromatic Compounds

Applied biocatalysis beyond just buffers – from aqueous to unconventional media. Options and guidelines

An In Vivo Biocatalytic Cascade Featuring an Artificial Enzyme Catalyzed New-to-Nature Reaction

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