Matteo Planchestainer


Last Name

Planchestainer

First Name

Matteo

ORCID

0000-0002-9938-5451

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2021 - 20253
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Publications 1 - 3 of 3
  • A microbial factory for bio-indigo synthesis: demonstration of sustainable denim dying
    Item type: Journal Article
    Planchestainer, Matteo; Chen, Lin; Kardashliev, Tsvetan; et al. (2025)
    Green Chemistry
    Biotechnological production using genetically engineered bacteria has the potential to enable environmentally friendly manufacturing of indigo without toxic intermediates or by-products, as in the case of traditional chemical processes. The shikimate and tryptophan pathways of Escherichia coli were engineered to supply a high level of the key intermediate indole, which was then converted to indigo by a naphthalene dioxygenase. The final strain yielded up to 12 g L$^{-1}$ of indigo dye under optimised cultivation conditions. The indigo was then purified using a sustainable process and used for dying of cotton fibers.
  • Late Microaerobic Growth for Efficient Production of Human Cytochrome P450 3A4 in E. coli
    Item type: Journal Article
    Marchetti, Luca; Planchestainer, Matteo; Panke, Sven; et al. (2023)
    Chimia
    Detailed preclinical characterization of metabolites formed in vivo from candidate drug substances is mandatory prior to the initiation of clinical trials. Therefore, inexpensive and efficient methods for drug metabolite synthesis are of high importance for rapid advancement of the drug development process. A large fraction of small molecule drugs is modified by monooxygenase cytochrome P450 3A4 produced in the human liver and intestine. Therefore, this enzyme is frequently employed to catalyze metabolite synthesis in vitro, making 3A4 availability a critical requirement in early drug development. Unfortunately, the recombinant production of this enzyme in microbial hosts is notoriously difficult. Maintaining low oxygen transfer rates and the use of rich media for host cultivation are required for P450 3A4 production. However, detailed studies on the relationship between oxygen supply and P450 3A4 space-time yields are missing. We describe an improved biotechnological process for the heterologous expression of P450 3A4 together with its redox partner, cytochrome P450 reductase, in Escherichia coli. Enzyme production was most efficient under so-called “late microaerobic” growth conditions, in which the cells have just not yet made the switch to anaerobic metabolism, characterized by a limited oxygen supply leading to oxygen concentrations in the liquid phase that are far below the detection limit of standard oxygen electrodes. Furthermore, feeding the carbon source glycerol as well as controlling cellular acetate formation improved process productivity. The presented protocol resulted in the formation of functional recombinant 3A4 at concentrations up to 680 nmol L⁻¹.
  • An alginate-confined peroxygenase-CLEA for styrene epoxidation
    Item type: Journal Article
    Nintzel, Friederike E. H.; Wu, Yinqi; Planchestainer, Matteo; et al. (2021)
    Chemical Communications
    Oxyfunctionalisation reactions in neat substrate still pose a challenge for biocatalysis. Here, we report an alginate-confined peroxygenase-CLEA to catalyse the enantioselective epoxidation of cis-β-methylstyrene in a solvent-free reaction system achieving turnover numbers of 96 000 for the biocatalyst and epoxide concentrations of 48 mM.
Publications 1 - 3 of 3