Immobilization of CalB Lipase by adsorption on magnetic nanoparticles: A heterogeneous biocatalysis/ Imobilização da lipase CalB por adsorção em nanopartículas magnéticas: um biocatalisador heterogêneo

Abstract

Iron magnetic nanoparticles (Fe3O4) were evaluated as adsorption preparative heterofunctional support for the immobilization of lipase B from Candida antarctica (CALB). Heterogeneous magnetic catalysts are easy to recover by the magnetic field, which may optimize operational cost and enhance the purity of the products. The nanoparticles were produced by the co-precipitation method. Modifications were carried out on the nanoparticles' surfaces with aminopropyltriethoxysilane (APTS). The adsorption was evaluated for 3.0 mg protein/g of support in the presence of 5mM sodium phosphate buffer, pH 7.0, at 25 °C and 0.5h of immobilization. In a solvent-free medium, under 37 °C, the biocatalyst prepared has shown activity of 2.2 U/g for the esterification of oleic acid after 0.5h, 37 kHz, and 300 W. The results obtained with CALB adsorbed onto magnetic iron nanoparticles were compared with those of lipase B from Candida antartica adsorbed onto acrylic resin (Novozym® 435). In this regard, under the same reactional conditions, Novozym® 435 has presented activity of 2.9 U/g.

A Convenient U-Shape Microreactor for Continuous Flow Biocatalysis with Enzyme-Coated Magnetic Nanoparticles-Lipase-Catalyzed Enantiomer Selective Acylation of 4-(Morpholin-4-yl)butan-2-ol

“…Candida antarctica lipase B (CaLB) has been also immobilized on hetero-functional MNPs by numerous methods, such as (i) adsorption on aminopropyltrimethoxysilane (ApTMOS)modified MNPs for kinetic resolution (KR) of secondary alcohols [39], on Lys-modified MNPs [40], on gallic acid-formaldehyde grafted MNPs [41], (ii) affinity binding of Histagged CaLB on magnetite MNPs containing long-armed nickel-nitrilotriacetic acid surface groups [42], or by (iii) covalent binding using diazonium chemistry for immobilization on carbon-coated MNPs [43], epoxy functionalized polymer-grafted MNPs [44], or (after glutaraldehyde activation) onto chitosan-coated MNPs [45,46], onto ApTMOS-activated MNPs [47][48][49][50], onto Lys-modified MNPs [40], and (iv) a combination of covalent attachment and polymer embedding onto MNPs [51]. The above-mentioned CaLB-MNP biocatalysts were already applied to produce short-and medium-chain fatty esters, employed as taste components [52], flavor esters [50,51,53], biodiesel [54], or to perform kinetic resolution of racemic secondary alcohols [39,46]. It was also shown that ultrasound agitation improves CaLB-MNPs activity [52].…”

“…The above-mentioned CaLB-MNP biocatalysts were already applied to produce short-and medium-chain fatty esters, employed as taste components [52], flavor esters [50,51,53], biodiesel [54], or to perform kinetic resolution of racemic secondary alcohols [39,46]. It was also shown that ultrasound agitation improves CaLB-MNPs activity [52].…”