ArticleMicrobial cell factories2012
Steroid biotransformations in biphasic systems with Yarrowia lipolytica expressing human liver cytochrome P450 genes.
Article in Microbial cell factories, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 53 citations in OpenAlex.
- Optimization of Human STARD3 Cholesterol Transporter Expression for Enhancing Bovine P450scc-Mediated Steroid Biotransformation in E. coli.Molecular biotechnology · 2026Article
- Using of transporter proteins to improve the uptake efficiency of hydrophobic compounds by Escherichia coli: a coordinated synthesis of START protein and P450scc system proteins to enhance cholesterol biotransformation.Bioresources and bioprocessing · 2025Article
- Functional expression and regulation of eukaryotic cytochrome P450 enzymes in surrogate microbial cell factories.Engineering microbiology · 2022Review
- Evolution and enrichment of CYP5035 in Polyporales: functionality of an understudied P450 family.Applied microbiology and biotechnology · 2021Article
- Review
- Investigation of Vitamin DChembiochem : a European journal of chemical biology · 2021Article
- Expanding the Diversity of Plant Monoterpenoid Indole Alkaloids Employing Human Cytochrome P450 3A4.Chembiochem : a European journal of chemical biology · 2020Article
- Metabolic Engineering of Oleaginous Yeasts for Production of Fuels and Chemicals.Frontiers in microbiology · 2017Review
- Versatile biocatalysis of fungal cytochrome P450 monooxygenases.Microbial cell factories · 2016Review
- Fungal cytochrome P450 monooxygenases of Fusarium oxysporum for the synthesis of ω-hydroxy fatty acids in engineered Saccharomyces cerevisiae.Microbial cell factories · 2015Article
- Yeast biotechnology: teaching the old dog new tricks.Microbial cell factories · 2014Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundYarrowia lipolytica efficiently metabolizes and assimilates hydrophobic compounds such as n-alkanes and fatty acids. Efficient substrate uptake is enabled by naturally secreted emulsifiers and a modified cell surface hydrophobicity and protrusions formed by this yeast. We were examining the potential of recombinant Y. lipolytica as a biocatalyst for the oxidation of hardly soluble hydrophobic steroids. Furthermore, two-liquid biphasic culture systems were evaluated to increase substrate availability. While cells, together with water soluble nutrients, are maintained in the aqueous phase, substrates and most of the products are contained in a second water-immiscible organic solvent phase.
resultsFor the first time we have co-expressed the human cytochromes P450 2D6 and 3A4 genes in Y. lipolytica together with human cytochrome P450 reductase (hCPR) or Y. lipolytica cytochrome P450 reductase (YlCPR). These whole-cell biocatalysts were used for the conversion of poorly soluble steroids in biphasic systems.Employing a biphasic system with the organic solvent and Y. lipolytica carbon source ethyl oleate for the whole-cell bioconversion of progesterone, the initial specific hydroxylation rate in a 1.5 L stirred tank bioreactor was further increased 2-fold. Furthermore, the product formation was significantly prolonged as compared to the aqueous system. Co-expression of the human CPR gene led to a 4-10-fold higher specific activity, compared to the co-overexpression of the native Y. lipolytica CPR gene. Multicopy transformants showed a 50-70-fold increase of activity as compared to single copy strains.
conclusionsAlkane-assimilating yeast Y. lipolytica, coupled with the described expression strategies, demonstrated its high potential for biotransformations of hydrophobic substrates in two-liquid biphasic systems. Especially organic solvents which can be efficiently taken up and/or metabolized by the cell might enable more efficient bioconversion as compared to aqueous systems and even enable simple, continuous or at least high yield long time processes.
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