Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials

Abstract

Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials Pavlidis, Ioannis V.; Vorhaben, Torge; Tsoufis, Theodoros; Rudolf, Petra; Bornscheuer, Uwe T.; Gournis, Dimitrios; Stamatis, Haralambos Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. a b s t r a c tIn this study we report the use of functionalized carbon-based nanomaterials, such as amine-functionalized graphene oxide (GO) and multi-walled carbon nanotubes (CNTs), as effective immobilization supports for various lipases and esterases of industrial interest. Structural and biochemical characterization have revealed that the curvature of the nanomaterial affect the immobilization yield, the catalytic behavior and the secondary structure of enzymes. Infrared spectroscopy study indicates that the catalytic behavior of the immobilized enzymes is correlated with their a-helical content. Hydrolases exhibit higher esterification activity (up to 20-fold) when immobilized on CNTs compared to GO. The covalently immobilized enzymes exhibited comparable or even higher activity compared to the physically adsorbed ones, while they presented higher operational stability. The enhanced catalytic behavior observed for most of the hydrolases covalently immobilized on amine-functionalized CNTs indicate that these functionalized nanomaterials are suitable for the development of efficient nanobiocatalytic systems.

Hybrid Nanomaterials of Magnetic Iron Nanoparticles and Graphene Oxide as Matrices for the Immobilization of β-Glucosidase: Synthesis, Characterization, and Biocatalytic Properties

“…It is expected that the structural characteristics of a nanomaterial, namely composition, size, surface area, functional groups and geometry, affect the immobilization yield, and the enzyme activity (Pavlidis et al, 2014). Moreover, the enzyme to support mass ratio could also affect the immobilization efficiency and the activity of immobilized enzymes (Pavlidis et al, 2012b;Samaratunga et al, 2015). In the present work, various enzyme to support mass ratios, ranging from 0.3 to 1.1, have been tested in order to optimize the immobilization yield and activity of bgl (data not shown).…”

“…It is interesting to note that bgl/GO-OA-γFe exhibits significant higher halflife constant than bgl/GO-γFe. The addition of the long alkyl chain of OA is expected to enhance the hydrophobic interactions between the nanosupports and the enzyme molecule, leading to a less flexible and thus more stable enzyme (Pavlidis et al, 2012b). …”

“…In biocatalysis, the development of novel nanobiocatalytic systems through the immobilization of enzymes on nanoscale materials attracted much scientific interest and their potential for applications in various industrial fields were recognized. The immobilization of enzymes on nano-sized materials leads to desirable nanobiocatalysts due to the higher enzyme loading capacity achieved, the enhanced mass transfer efficiency, and the stabilization that nanomaterials provide (Pavlidis et al, 2012b;Patila et al, 2016b).…”

In situ synthesized rGO–Fe3O4 nanocomposites as enzyme immobilization support for achieving high activity recovery and easy recycling

“…It is one of the most important strategies to explore the feasible and effective supports for enhancing the catalytic performance of immobilized enzymes. Recently, with the rapid development of nanotechnology, the nano−supports, i.e., using nanomaterials as the supports for enzyme immobilization, are becoming more and more attractive owing to their large specific surface area, controllable size at the nanometer scale, and similar size with enzyme molecules [4][5][6].…”

Recent progress in nanobiocatalysis for enzyme immobilization and its application

“…Various lipases and esterases were also immobilized on the aminefunctionalized graphene oxide and MWNT with glutaraldehyde as a cross-linking reagent. The structural and the biochemical characterization were conducted, and consequently it was validated that the curvature of the nanomaterial affected the immobilization yield, the catalytic behavior, and the secondary structure of the enzyme [15]. Dyal et al also developed a strategy for the immobilized enzyme on the γ-Fe 2 O 3 magnetic nanoparticles by introducing acetylated-or amine-functionalization, as shown in Fig.…”