ArticleApplied and environmental microbiology2012
Outer membrane protein AlkL boosts biocatalytic oxyfunctionalization of hydrophobic substrates in Escherichia coli.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 121 citations in OpenAlex.
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- De novo biosynthesis of nylon 12 monomer ω-aminododecanoic acid.Nature communications · 2025Article
- Assimilation of phthalate esters in bacteria.Applied microbiology and biotechnology · 2024Review
- Strategies found not to be suitable for stabilizing high steroid hydroxylation activities of CYP450 BM3-based whole-cell biocatalysts.PloS one · 2024Article
- Structure and Function of Alkane Monooxygenase (AlkB).Accounts of chemical research · 2023Review
- Engineering caveolin-mediated endocytosis inSynthetic and systems biotechnology · 2022Article
- Spheroplasts preparation boosts the catalytic potential of a squalene-hopene cyclase.Nature communications · 2022Article
- α-Dioxygenases (α-DOXs): Promising Biocatalysts for the Environmentally Friendly Production of Aroma Compounds.Chembiochem : a European journal of chemical biology · 2022Review
- Whole cells of recombinant CYP153A6-E. coli as biocatalyst for regioselective hydroxylation of monoterpenes.AMB Express · 2022Article
- Efficient Synthesis of (Frontiers in bioengineering and biotechnology · 2022Article
- An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB).Frontiers in microbiology · 2022Review
- When metabolic prowess is too much of a good thing: how carbon catabolite repression and metabolic versatility impede production of esterified α,ω-diols in Pseudomonas putida KT2440.Biotechnology for biofuels · 2021Article
- The Transporter-Mediated Cellular Uptake and Efflux of Pharmaceutical Drugs and Biotechnology Products: How and Why Phospholipid Bilayer Transport Is Negligible in Real Biomembranes.Molecules (Basel, Switzerland) · 2021Review
- Investigation of the prevalence and catalytic activity of rubredoxin-fused alkane monooxygenases (AlkBs).Journal of inorganic biochemistry · 2021Article
- One-pot synthesis of 6-aminohexanoic acid from cyclohexane using mixed-species cultures.Microbial biotechnology · 2021Article
- Comparative Proteomics ofMicroorganisms · 2020Article
- A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Process intensification for cytochrome P450 BM3-catalyzed oxy-functionalization of dodecanoic acid.Biotechnology and bioengineering · 2020Article
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The outer membrane of microbial cells forms an effective barrier for hydrophobic compounds, potentially causing an uptake limitation for hydrophobic substrates. Low bioconversion activities (1.9 U g(cdw)(-1)) have been observed for the ω-oxyfunctionalization of dodecanoic acid methyl ester by recombinant Escherichia coli containing the alkane monooxygenase AlkBGT of Pseudomonas putida GPo1. Using fatty acid methyl ester oxygenation as the model reaction, this study investigated strategies to improve bacterial uptake of hydrophobic substrates. Admixture of surfactants and cosolvents to improve substrate solubilization did not result in increased oxygenation rates. Addition of EDTA increased the initial dodecanoic acid methyl ester oxygenation activity 2.8-fold. The use of recombinant Pseudomonas fluorescens CHA0 instead of E. coli resulted in a similar activity increase. However, substrate mass transfer into cells was still found to be limiting. Remarkably, the coexpression of the alkL gene of P. putida GPo1 encoding an outer membrane protein with so-far-unknown function increased the dodecanoic acid methyl ester oxygenation activity of recombinant E. coli 28-fold. In a two-liquid-phase bioreactor setup, a 62-fold increase to a maximal activity of 87 U g(cdw)(-1) was achieved, enabling the accumulation of high titers of terminally oxyfunctionalized products. Coexpression of alkL also increased oxygenation activities toward the natural AlkBGT substrates octane and nonane, showing for the first time clear evidence for a prominent role of AlkL in alkane degradation. This study demonstrates that AlkL is an efficient tool to boost productivities of whole-cell biotransformations involving hydrophobic aliphatic substrates and thus has potential for broad applicability.
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