PdNP bionanohybrid catalyzed selective C–H bond arylation of tryptophan residues in proteins in aqueous media at room temperature.

This review describes the advances in the design and application of novel artificial metalloenzymes in C–H activation reactions.

Applied nanotechnology has experienced tremendous advance over the last decade. In this study, the efficient synthesis of highly stable palladium-nanoparticles (PdNPs) biohybrids based on the application of an enzyme, which induces in situ the generation of spherical nanoparticles on the protein network, has been described. A heterogeneous material was synthesized formed with PdNPs with average sizes between 1.5 to 5 nm. These Pd nanocatalysts were successfully applied in different chemical processes: C-C bonding reactions (Suzuki and Heck reactions) and cascade processes combining enzymatic and metallic activities (hydrolysis-reduction, esterification-racemization).

Full degradation of p-aminophenol in aqueous solution at room temperature by using a heterogeneous nanostructured iron hybrid catalyst in the presence of hydrogen peroxide is described. A nanostructured iron catalyst was prepared by in situ formation of iron carbonate nanorods on the protein network using an aqueous solution of an enzyme, lipase B from Candida antarctica (CAL-B). A second kind of iron nanostructured catalyst was obtained by the sunsequent treatment of the hybrid with an aqueous liquid extract of Mentha x piperita. Remarkable differences were observed using TEM imaging. When M. piperita extract was used, nanoparticles appeared instead of nanorods. Catalytic activity of these iron nanocatalysts was studied in the degradation of the environmental pollutant p-aminophenol (pAP) under different operating parameters, such as pH, presence of buffer or hydrogen peroxide concentration. Optimal conditions were pH 4 in acetate buffer 10 mM containing 1% (v/v) H₂O₂ for FeCO₃NRs@CALB, while for FeCO₃NRs@CALB-Mentha, water containing 1% (v/v) H₂O₂, resulted the best. A complete degradation of 100 ppm of pAP was achieved in 2 and 3 min respectively using 1 g Fe/L. This novel nanocatalyst was recycled five times maintaining full catalytic performance.

The application of novel methodologies to the synthesis of nanomaterials is still a challenge in many different technological and scientific fields. New efficient and reproducible synthetic methodologies, that produce fewer residues and reduce the cost of raw materials must be developed. In the present work, we have explored the attractive possibility to apply the cheap iron (II) sulphate salt in the reduction process of the K₂PtCl₄ to produce colloids suspensions. The synthesis took places in water and was assisted by sodium citrate (SC) using polyvinylpyrrolidone (PVP) as a surfactant. The adjustment of this novelty process allows obtaining well-dispersed and sub-20 nm dendrimer-type platinum nanoparticles (Pt D-NPs). The nano-dendrimers produced have been characterized using dynamic light scattering (DLS), transmission electron microscopy (TEM), high-resolution TEM (HR-TEM), XRD spectroscopy, inductive couple plasma (ICP) analysis, Fourier transform infrared (FT-IR) and ultraviolet-visible (UV-vis) spectroscopy. Interesting conformational results derived from the size and shape will be discussed. Catalytic application of the Pt D-NPs has been explored in the reduction of p-nitrophenol (p-NP) to p-aminophenol (p-AP) in aqueous media at room temperature obtained TOF value of 253 min^-1. Finally, our Pt D-NPs were tested as artificial metalloenzyme showing catechol oxidase activity for oxidation of L-DOPA. Open image in new window

Three novel glycosidases produced from Lactobacillus plantarum, so called Lp_0440, Lp_2777, and Lp_3525, were isolated and overexpressed on Escherichia coli containing a His-tag for specific purification. Their specific activity was evaluated against the hydrolysis of p-nitrophenylglycosides and p-nitrophenyl-6-phosphate glycosides (glucose and galactose) at pH 7. All three were modified with hyaluronic acid (HA) following two strategies: A simple coating by direct incubation at alkaline pH or direct chemical modification at pH 6.8 through preactivation of HA with carbodiimide (EDC) and N-hydroxysuccinimide (NHS) at pH 4.8. The modifications exhibited important effect on enzyme activity and specificity against different glycopyranosides in the three cases. Physical modification showed a radical decrease in specific activity on all glycosidases, without any significant change in enzyme specificity toward monosaccharide (glucose or galactose) or glycoside (C-6 position free or phosphorylated). However, the surface covalent modification of the enzymes showed very interesting results. The glycosidase Lp_0440 showed low glycoside specificity at 25 °C, showing the same activity against p-nitrophenyl-glucopyranoside (pNP-Glu) or p-nitrophenyl-6-phosphate glucopyranoside (pNP-6P-Glu). However, the conjugated cHA-Lp_0440 showed a clear increase in the specificity towards the pNP-Glu and no activity against pNP-6P-Glu. The other two glycosidases (Lp_2777 and Lp_3525) showed high specificity towards pNP-6P-glycosides, especially to the glucose derivative. The HA covalent modification of Lp_3525 (cHA-Lp_3525) generated an enzyme completely specific against the pNP-6P-Glu (phosphoglycosidase) maintaining more than 80% of the activity after chemical modification. When the temperature was increased, an alteration of selectivity was observed. Lp_0440 and cHA-Lp_0440 only showed activity against p-nitrophenyl-galactopyranoside (pNP-Gal) at 40 °C, higher than at 25 °C in the case of the conjugated enzyme.