1. Lipase immobilized on magnetic hierarchically porous carbon materials as a versatile tool for the synthesis of bioactive quercetin derivatives
- Author
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Michaela Patila, Alexandra V. Chatzikonstantinou, Eleni Thomou, Nikolaos Chalmpes, Angeliki C. Polydera, Konstantinos Spyrou, Luiz Estevez, Emmanuel P. Giannelis, Dimitrios Gournis, Mohamed Amen Hammami, Turki N. Baroud, Haralambos Stamatis, Apostolos Enotiadis, and Andreas G. Tzakos
- Subjects
Environmental Engineering ,Nanostructure ,Immobilized enzyme ,biology ,Renewable Energy, Sustainability and the Environment ,Chemistry ,020209 energy ,Bioengineering ,02 engineering and technology ,010501 environmental sciences ,01 natural sciences ,Combinatorial chemistry ,Catalysis ,chemistry.chemical_compound ,Biocatalysis ,0202 electrical engineering, electronic engineering, information engineering ,biology.protein ,Lipase ,Bioprocess ,Quercetin ,Waste Management and Disposal ,Derivative (chemistry) ,0105 earth and related environmental sciences - Abstract
The preparation, characterization and application of a novel robust nanobiocatalyst, developed through the covalent binding of lipase B from Pseudozyma antarctica on magnetic hierarchically porous carbon materials (HPCFe), is reported. The nanobiocatalyst was characterized by combination of spectroscopic and microscopic techniques. Structural and catalytic characterization indicates that HPCFe nanostructures create a microenvironment which stabilizes the structure of the immobilized enzyme, resulting in enhanced activity and stability in non-aqueous media over other forms of the biocatalyst. The nanobiocatalyst was effectively applied for the selective deacetylation of peracetylated quercetin towards the synthesis of 3,5,7-triacetoxy-3′,4′-dihydroxyflavone, a compound with high antiproliferative activity. At the optimum bioprocess conditions, the produced amount of the bioactive quercetin derivative in a single-step process reached values up to 3.48 g L−1 which is 13 times higher than that reported to date. The immobilized enzyme retains ~100% of its catalytic activity after 10 repeated reaction cycles.
- Published
- 2020