Lipase immobilized on magnetic hierarchically porous carbon materials as a versatile tool for the synthesis of bioactive quercetin derivatives

March 24, 2020

Title

Lipase immobilized on magnetic hierarchically porous carbon materials as a versatile tool for the synthesis of bioactive quercetin derivatives

Author

Alexandra V. Chatzikonstantinou, Angeliki C. Polydera, Eleni Thomou, Nikolaos Chalmpes, Turki N. Baroud, Apostolos Enotiadis, Luiz Estevez, Michaela Patila, Mohamed Amen Hammami, Konstantinos Spyrou, Emmanuel P. Giannelis, Andreas G. Tzakos, Dimitrios Gournis, Haralambos Stamati

Year

2020

Journal

Bioresource Technology Reports

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.

Instrument

J-1500

Keywords

Circular dichroism, Secondary structure, Protein folding, Chemical stability, Nanostructures, Materials, Biochemistry