Lipase immobilized on magnetic hierarchically porous carbon materials as a versatile tool for the synthesis of bioactive quercetin derivatives. (February 2020)

• Record Type: Journal Article
• Authors: Chatzikonstantinou, Alexandra V.; Polydera, Angeliki C.; Thomou, Eleni; Chalmpes, Nikolaos; Baroud, Turki N.; Enotiadis, Apostolos; Estevez, Luiz; Patila, Michaela; Hammami, Mohamed Amen; Spyrou, Konstantinos; Giannelis, Emmanuel P.; Tzakos, Andreas G.; Gournis, Dimitrios; Stamatis, Haralambos
• Is Part Of: Bioresource technology reports. Volume 9(2020)
• Publication Date: 2020-02
• Subjects: Porous magnetic nanomaterials -- Lipase B -- Immobilization -- Nanobiocatalysis -- Quercetin acetyl analogues; Biomass energy -- Periodicals; Biotransformation (Metabolism) -- Periodicals; Agricultural wastes -- Periodicals; Factory and trade waste -- Periodicals; Organic wastes -- Periodicals; Waste products as fuel -- Periodicals; Waste products as fuel; Organic wastes; Factory and trade waste; Biotransformation (Metabolism); Biomass energy; Agricultural wastes; Periodicals; Electronic journals; 662.88
• DOI: 10.1016/j.biteb.2019.100372
• Languages: English
• ISSNs: 2589-014X

Abstract

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. Graphical abstract: Unlabelled Image Highlights: Lipase immobilization on magnetic hierarchically porous carbon materials. Synthesis of bioactive quercetin derivatives by magnetic nanobiocatalyst. HPCFe hybrids create a microenvironment which stabilizes the enzyme structure. The novel magnetic nanobiocatalyst exhibited excellent operational stability.