0000000000133879

AUTHOR

Luca Ronda

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
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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
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Hemocyanin from E. californicum encapsulated in silica gels: oxygen binding and conformational states.

2007

Cooperativity depends on the existence of equilibria among functionally distinct conformational states that are affected by homo and heterotropic effectors. In order to isolate the quaternary conformations of hemocyanin from E. californicum, the 24-meric giant protein was encapsulated in wet, nanoporous silica gels, either in the absence or presence of oxygen. The deoxy- and oxy-hemocyanin gels exhibit a p50 for oxygen of 11 and 2.5 torr, respectively, values in close agreement with those for hemocyanin in solution. The observed Hill coefficients are lower than unity, indicating a conformational heterogeneity within each locked conformational state, a finding in agreement with the assumptio…

Models MolecularAbsorption spectroscopyProtein Conformationmedicine.medical_treatmentchemistry.chemical_elementCooperativityBiologyOxygenGeneticsmedicineAnimalsNanoporousHemocyaninSpidersGeneral MedicineSilicon DioxideOxygenSolutionsCrystallographyKineticsBiochemistrychemistrySpectrophotometryHemocyaninsHemoglobinGelsOxygen bindingAlgorithmsProtein BindingGene
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