Robust Light Driven Enzymatic Oxyfunctionalization via Immobilization of Unspecific Peroxygenase.

Unspecific peroxygenases have attracted interest in synthetic chemistry, especially for the oxidative activation of C-H bonds, as they only require hydrogen peroxide (H O ) instead of a cofactor. Due to their instability in even small amounts of H O , different strategies like enzyme immobilization or in situ H O production have been developed to improve the stability of these enzymes. While most strategies have been studied separately, a combination of photocatalysis with immobilized enzymes was only recently reported.

Synthesis of silver and gold nanoparticles-enzyme-polymer conjugate hybrids as dual-activity catalysts for chemoenzymatic cascade reactions.

Novel hybrids containing silver or gold nanoparticles have been synthesized in aqueous media and at room temperature using enzymes or tailor-made enzyme-polymer conjugates, which directly induced the formation of inorganic silver or gold species. The choice of pH, protein, or bioconjugate strongly affected the final metallic nanoparticles hybrid formation. Using (CALB) in a solution, nanobiohybrids containing AgO nanoparticles of 9 nm average diameter were obtained.

Pd-Oxazolone complexes conjugated to an engineered enzyme: improving fluorescence and catalytic properties.

Different Pd-complexes containing orthometallated push-pull oxazolones were inserted by supramolecular Pd-amino acid coordination on two genetically engineered modified variants of the thermoalkalophilic Geobacillus thermocatenolatus lipase (GTL). Pd-lipase conjugation was performed on the solid phase in the previously immobilized form of GTL under mild conditions, and soluble conjugated Pd-GTL complexes were obtained by simply desorbing by washing with an acetonitrile aqueous solution. Three different Pd complexes were incorporated into two different genetically modified enzyme variants, one containing all the natural cysteine residues changed to serine residues, and another variant including an additional Cys mutation directly in the catalytic serine (Ser114Cys).

Microbial lipase: a new approach for a heterogeneous biocatalyst.

Lipases are enzymes employed in several industrial process and their applicability can be increased if these biocatalysts are in the immobilize form. The objective of this work was to study the immobilization of lipase produced by submerged cultivation of sp. by hydrophobic interaction, evaluating its stability and reuse capacity.

The enzyme-induced formation of iron hybrid nanostructures with different morphologies.

A new synthesis method for tailor-made iron-hybrid nanoparticles has been carried out for the first time using enzymes, which directly induce the formation of inorganic iron species. The role of the protein was critical for the formation and morphology of the iron nanostructures and, depending on the enzyme, by simple mixing with ammonium iron(ii) sulfate at room temperature and under air, it was possible to obtain, for the first time, well stabilized superparamagnetic iron and iron oxide nanorods, nanosheets and nanorings or even completely amorphous non-magnetic iron structures in the protein network. These iron nanostructure-enzyme hybrids showed excellent results as heterogeneous catalysts in organic chemistry (chemoselective hydrogenation and C-C bonding formation) and environmental remediation processes.

Site-selective modification of tryptophan and protein tryptophan residues through PdNP bionanohybrid-catalysed C-H activation in aqueous media.

Herein we report for the first time the site-selective C-H bond arylation of tryptophan and tryptophan residues in proteins in aqueous media at room temperature by using a PdNP bionanohybrid as a heterogeneous catalyst. The reaction proceeds using a stable aryldiazonium salt without a base.

Synthesis of a superparamagnetic ultrathin FeCO nanorods-enzyme bionanohybrid as a novel heterogeneous catalyst.

Herein we report a straightforward synthesis of an ultrathin protein-iron(ii) carbonate nanorods (FeCO3-NRs) heterogeneous bionanohybrid at room temperature and in aqueous media. The enzyme induced the in situ formation of well-dispersed FeCO3 NRs on a protein network. The addition of NaBH4 as a reducing agent allowed us to obtain nanorods (5 × 40 nm) with superparamagnetic properties.