Continuous Fatty Acid Decarboxylation using an Immobilized Photodecarboxylase in a Membrane Reactor

ChemSusChem, Journal Year: 2023, Volume and Issue: 17(3)

Published: Nov. 21, 2023

The realm of photobiocatalytic alkane biofuel synthesis has burgeoned recently; however, the current dearth well-established and scalable production methodologies in this domain remains conspicuous. In investigation, we engineered a modified form membrane-associated fatty acid photodecarboxylase sourced from Micractinium conductrix (McFAP). This endeavour resulted creating an innovative assembled photoenzyme-membrane (protein load 5 mg cm

Language: Английский

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Photodecarboxylase Displayed on Microbial Cell‐Surface for Enhanced Biocatalytic Performance

ChemCatChem, Journal Year: 2023, Volume and Issue: 15(14)

Published: May 22, 2023

Abstract Surface display technology has emerged as a powerful tool for enhancing the stability, accessibility, and reusability of enzymes. Fatty acid photodecarboxylase from Chlorella variabilis NC64A ( Cv FAP) is capable catalyzing decarboxylation reactions free fatty acids to alkanes under blue light, however, its stability in catalytic cycles remain be improved. Herein, we successfully displayed FAP on surface Escherichia coli cells utilizing full‐length ice nucleation protein anchor protein. By comparing performance with whole‐cells harboring FAP, it was found that displaying significantly reduces reaction time enhances substrate resulting turnover number 9972. Also, compared soluble enzymes, exhibits enhanced reaction. Furthermore, broad scope suggests potential large‐scale hydrocarbon chemicals production. Overall, our results highlight value approach broadening application photodecarboxylase.

Language: Английский

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Strategies towards sustainable synthetic routes to deuterium-labelled organic compounds using immobilized and recyclable (bio)catalysts

Green Synthesis and Catalysis, Journal Year: 2024, Volume and Issue: unknown

Published: Oct. 1, 2024

Language: Английский

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Microbial photoproduction of heptane

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: July 19, 2024

Abstract Fatty Acid Photodecarboxylase (FAP) has emerged as a promising catalyst for the biological production of long-chain hydrocarbons. We have recently shown that purified FAP or FAP-expressing bacteria can efficiently convert octanoic acid into heptane, thus extending potential applications to medium-chain hydrocarbons (i.e., solvent- kerosene-type). The scarcity natural sources presents challenge however. Here, we explore heptane capacity E. coli strain engineered biosynthesize via specific thioesterase. Various FAPs and C8-specific thioesterases were tested. A blue-light-inducible promoter was used avoid chemical inducers. found expression fused with TrxA resulted in 10-fold increase production. Coexpression Cuphea hookeriana thioesterase Chlorella variabilis achieved highest titer (12.5 mg.L -1 ). Scale-up experiments 100 mL photobioreactors allowed constant over two days (22 .day Graphical Highlights An producing under blue light is described. Expression increases by 10-fold. light-inducible ensures high coexpression give Highest reported productivity ) photobioreactors.

Language: Английский

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Active-Site Mutagenesis of Fatty Acid Photodecarboxylase: Experimental and Computational Insight into Substrate Chain-Length Specificity

ACS Catalysis, Journal Year: 2024, Volume and Issue: 14(21), P. 15837 - 15849

Published: Oct. 10, 2024

Fatty acid photodecarboxylase (FAP), a microalgal enzyme, is one of the rare photoenzymes found in nature. Since its discovery 2017, FAP has made huge impact field photobiocatalysis, being so far only photoenzyme with potential applicability for organic synthesis. Furthermore, among all studied enzymes to date, most promising candidates vitro feasible biofuel production from oil. One study been broadening substrate scope and modulating selectivity. In order get insight into enzyme's selectivity, as well generate toolbox mutant distinct preferences toward medium- long-chain fatty acids, this work, we carried out extensive mutagenesis active-site residues Chlorella variabilis (CvFAP). Particularly, performed partial-site saturation Y466 position due key location at active site. Our experimental computational analysis indicated correlation between exchanged amino type observed activity, demonstrating that conventional binding mode acids destabilized by charged residues, leading nonproductive conformation characterized compact folded form. Mutagenesis other around site led variants selectivity medium-chain or acids. For example, obtained enzyme are highly selective either C12:0, C14:0, C18:0/C18:1 Selectivity patterns agreed very distances FAD cofactor substrate, calculated our molecular dynamics simulations. report unexplored activity wild-type CvFAP C20:1 C22:1 which major components jojoba oil rapeseed oil, respectively.

Language: Английский

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Photoenzymatic Catalysis for Organic Synthesis

Elsevier eBooks, Journal Year: 2023, Volume and Issue: unknown, P. 143 - 177

Published: Sept. 25, 2023

Language: Английский

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