High load drug release systems based on carbon porous nanocapsule carriers. Ibuprofen case study.

This work shows the application of carbon nanocapsules as carriers for sodium ibuprofen release. Hard templating was used to prepare spherical carbon nanocapsules (mean diameter and thick shell of 690 and 70 nm, respectively), exhibiting both micro and mesoporosity. For comparison purposes, a microporous commercial activated carbon and a home-made mesoporous CMK-3 were also studied.

Very Strong but Reversible Immobilization of Enzymes on Supports Coated with Ionic Polymers.

In this chapter, the properties of tailor-made anionic exchanger resins based on films of large polyethylenimine polymers (e.g., molecular weight 25,000) as supports for strong but reversible immobilization of proteins are shown.

Encapsulation of Ionic Liquids with an Aprotic Heterocyclic Anion (AHA-IL) for CO Capture: Preserving the Favorable Thermodynamics and Enhancing the Kinetics of Absorption.

The performance of an ionic liquid with an aprotic heterocyclic anion (AHA-IL), trihexyl(tetradecyl)phosphonium 2-cyanopyrrolide ([P][2-CNPyr]), for CO capture has been evaluated considering both the thermodynamics and the kinetics of the phenomena. Absorption gravimetric measurements of the gas-liquid equilibrium isotherms of CO-AHA-IL systems were carried out from 298 to 333 K and at pressures up to 15 bar, analyzing the role of both chemical and physical absorption phenomena in the overall CO solubility in the AHA-IL, as has been done previously. In addition, the kinetics of the CO chemical absorption process was evaluated by in situ Fourier transform infrared spectroscopy-attenuated total reflection, following the characteristic vibrational signals of the reactants and products over the reaction time.

Encapsulated ionic liquids (ENILs): from continuous to discrete liquid phase.

Encapsulated ionic liquid (ENIL) material was developed, consisting of ionic liquid (IL) introduced into carbon submicrocapsules. ENILs contain >85% w/w of IL but discretized in submicroscopic encapsulated drops, drastically increasing the surface contact area with respect to the neat fluid. ENIL materials were here tested for gas separation processes, obtaining a drastic increase in mass transfer rate.

Preparation of a very stable immobilized biocatalyst of glucose oxidase from Aspergillus niger.

Glucose oxidase (GOX) has been immobilized on different activated supports, including glyoxyl agarose, epoxy sepabeads and glutaraldehyde-activated supports. Immobilization onto supports pre-activated with glutaraldehyde rendered the most thermo-stable preparation of GOX. Therefore, as the glutaraldehyde chemistry gave a high stabilization of the enzyme, we proposed another technique for improving the multipoint attachment through glutaraldehyde: the enzyme was ionically adsorbed on cationic supports with primary amino groups and then the immobilized preparation was treated with a glutaraldehyde solution.

Enzyme stabilization by glutaraldehyde crosslinking of adsorbed proteins on aminated supports.

The stabilization achieved by different immobilization protocols have been compared using three different enzymes (glutaryl acylase (GAC), D-aminoacid oxidase (DAAO), and glucose oxidase (GOX)): adsorption on aminated supports, treatment of this adsorbed enzymes with glutaraldehyde, and immobilization on glutaraldehyde pre-activated supports. In all cases, the treatment of adsorbed enzymes on amino-supports with glutaraldehyde yielded the higher stabilizations: in the case of GOX, a stabilization over 400-fold was achieved. After this treatment, the enzymes could no longer be desorbed from the supports using high ionic strength (suggesting the support-protein reaction).

Prevention of interfacial inactivation of enzymes by coating the enzyme surface with dextran-aldehyde.

Interactions between soluble enzymes and interfaces of organic solvent drops or gas bubbles have a very negative effect on the operational stability of the soluble enzymes. In this study, the formation of a hydrophilic shell around the enzyme has been attempted using dextran-aldehyde which would prevent the interaction between enzyme and hydrophobic interfaces with minimal modification of the enzyme surface. After optimizing the size of the dextran (that was found to play a critical role), three different enzymes (glucose oxidase, d-amino acid oxidase, and trypsin) have been conjugated with dextran-aldehyde and their stability towards organic-aqueous and air-liquid interfaces has been evaluated.

Reversible immobilization of glutaryl acylase on sepabeads coated with polyethyleneimine.

The immobilizaton of the enzyme glutaryl-7-aminocephalosporanic acid acylase (GA) was performed via ionic adsorption onto several supports: a new anionic exchange resin, based on the coating of Sepabeads internal surfaces with polyethyleneimine (PEI) of different molecular weights, and conventional EC-Q1A-Sepabeads and DEAE-agarose. Immobilization occurred very rapidly in all cases, but the adsorption strength was much higher in the case of PEI-Sepabeads than in the other supports at pH 7 (e.g.