Abstract
Elongated flexuous plant viral nanoparticles (VNPs) represent an interesting platform for developing different applications in nanobiotechnology. In the case of potyviruses, the virion external surface is made up of helically arrayed domains of the viral structural coat protein (CP), repeated over 2000 times, in which the N- and C-terminal domains of each CP are projected toward the exterior of the external virion surface. These characteristics provide a chemical environment rich in functional groups susceptible to chemical conjugations. We have conjugated Candida antarctica lipase B (CALB) onto amino groups of the external surface of the potyvirus turnip mosaic virus (TuMV) using glutaraldehyde as a conjugating agent. Using this approach, TuMV virions were transformed into scaffolds for CALB nanoimmobilization. Analysis of the resulting structures revealed the formation of TuMV nanonets onto which large CALB aggregates were deposited. The functional enzymatic characterization of the CALB-bearing TuMV nanonets showed that CALB continued to be active in the nanoimmobilized form, even gaining an increased relative specific activity, as compared to the non-immobilized form. These novel virus-based nanostructures may provide a useful new approach to enzyme nanoimmobilization susceptible to be industrially exploited.
Highlights
Enzyme immobilization is a common practice widely adopted in many industrial biochemical processes (DiCosimo et al, 2013; Sheldon and van Pelt, 2013)
The ratio increase observed at pH 5.0 and pH 12.0 was evident when whole UV spectra were obtained at varying pH values (Supplementary Figure S1). These results are consistent with the assertion that chemical conjugations performed in the 6.0–11.0 pH range do not affect overall virion structure
Given the presence of amines on the surfaces of both Candida antarctica lipase B (CALB) and the turnip mosaic virus (TuMV) coat protein (CP), the components of the complex nanonets are, presumably, covalently linked via imine formation mediated by the GA
Summary
Enzyme immobilization is a common practice widely adopted in many industrial biochemical processes (DiCosimo et al, 2013; Sheldon and van Pelt, 2013). Immobilized enzymes can provide additional advantages like an increased resistance to potential factors that stress enzymatic activity, for instance pH, pressure, temperature or solute concentrations (Mateo et al, 2007; Branco et al, 2015). Notwithstanding the clear advantages, Enzyme Immobilization on Viral Nanonets immobilization processes often take place with an associated loss of enzyme specific activity (Sheldon and van Pelt, 2013). This undesirable side effect may result from protein rigidity or lack of mobility imposed by enzyme immobilization. The overall advantages are superior to the disadvantages, and use of immobilized enzymes continues to increase
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