0000000000133882

AUTHOR

Barbara Campanini

0000-0003-0359-0627

showing 3 related works from this author

More than a Confinement: “Soft” and “Hard” Enzyme Entrapment Modulates Biological Catalyst Function

2019

Catalysis makes chemical and biochemical reactions kinetically accessible. From a technological point of view, organic, inorganic, and biochemical catalysis is relevant for several applications, from industrial synthesis to biomedical, material, and food sciences. A heterogeneous catalyst, i.e., a catalyst confined in a different phase with respect to the reagents’ phase, requires either its physical confinement in an immobilization matrix or its physical adsorption on a surface. In this review, we will focus on the immobilization of biological catalysts, i.e., enzymes, by comparing hard and soft immobilization matrices and their effect on the modulation of the catalysts’ function. Indeed, …

inorganic chemicals02 engineering and technology010402 general chemistryHeterogeneous catalysisbiosensor01 natural sciencesCatalysischemistry.chemical_compoundbioreactorAdsorptionBioreactorMoleculePhysical and Theoretical ChemistrytrehalosecatalysisSilica gelsilica gel021001 nanoscience & nanotechnology0104 chemical sciencesenzymeChemical engineeringchemistryReagentencapsulation0210 nano-technologyBiosensor
researchProduct

Immobilization of proteins in silica gel: Biochemical and biophysical properties

2015

The development of silica-based sol-gel techniques compatible with the retention of protein structure and function started more than 20 years ago, mainly for the design of biotechnological devices or biomedical applications. Silica gels are optically transparent, exhibit good mechanical stability, are manufactured with different geometries, and are easily separated from the reaction media. Biomolecules encapsulated in silica gel normally retain their structural and functional properties, are stabilized with respect to chemical and physical insults, and can sometimes exhibit enhanced activity in comparison to the soluble form. This review briefly describes the chemistry of protein encapsulat…

protein dynamicsol-gel; encapsulation; biophysics; protein dynamics; heme proteinsOrganic Chemistrysol-gelencapsulationConformational transitionsProtein dynamicsbiophysicSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)heme proteins
researchProduct

GFP-mut2 Proteins in Trehalose-Water Matrixes: Spatially Heterogeneous Protein-Water-Sugar Structures

2007

We report investigations on the properties of nanoenvironments around single-GFP-mut2 proteins in trehalose-water matrixes. Single-GFPmut2 molecules embedded in thin trehalose-water films were characterized in terms of their fluorescence brightness, bleaching dynamics, excited state lifetime, and fluorescence polarization. For each property, sets of approximately 100-150 single molecules have been investigated as a function of trehalose content and hydration. Three distinct and interconverting families of proteins have been found which differ widely in terms of bleaching dynamics, brightness, and fluorescence polarization, whose relative populations sizably depend on sample hydration. The r…

Green Fluorescent ProteinsBiophysicsAnalytical chemistryCarbohydratesMolecular ConformationPhase TransitionColloidchemistry.chemical_compoundMoleculeColloidsSupercoolingthrealosesingle molecule fluorescenceChemistryTrehaloseWaterSingle-molecule experimentFluorescenceTrehaloseSolutionsModels ChemicalChemical physicsCell BiophysicsGFPmut2Excited statelifetimesFluorescence anisotropy
researchProduct