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The synthesis, as well as the spectroscopic and structural characterization of three analogous palladium(II) complexes, [Pd{(Ph2P)2N(tBu)-κ2P,P´}X2], X = Cl, Br, I, is presented. X-ray crystallography studies revealed a similar square planar PdP2X2 first coordination sphere among the three complexes. The catalytic reactivity of these complexes was tested in the Suzuki-Miyaura coupling reaction, showing that the X = Cl, Br, complexes are more active than the X = I analogue. The differences in the catalytic reactivity within this series of complexes, as well as comparisons with similar palladium(II) catalysts reported in the literature, are discussed with respect to the different electronegativity of the three halogens and the strong +I inductive effect of the ligand's tBu group.

Lipase from Mucor miehei was immobilized on chitosan hydrogels without using any activation agent. These low-cost and easy to prepare lipase-containing hydrogels could be considered as novel solid-phase biocatalysts for use in organic media. When they were applied as biocatalysts towards the model esterification reaction of propyl laurate synthesis they showed an optimum operation temperature at 30 °C and maintained a high catalytic activity in various non-polar organic solvents. The higher initial esterification rates were obtained when biocatalysis took place in branched hydrocarbons where the initial rates recorded were twice the ones observed for straight hydrocarbons, being 0.22 mM/min in isooctane and 0.11 mM/min in hexane, respectively. The novel catalyst presented excellent reusability, with only 10% loss of activity after 12 uses, which is even higher than the one obtained by lipase-containing chitosan beads prepared with a cross-linker. Moreover, enzyme superactivity was evident for several runs.

Weak self-assembly systems consisted by a nonpolar hydrocarbon, an alcohol and water can form macroscopically homogeneous liquid media with distinct microenvironments of varying polarity. These ternary systems are very similar to classic water in oil microemulsions although they don't have any amphiphilic surfactant. They were thus, initially called “surfactantless” or “detergentless” microemulsions. One of the main application fields that these systems cover is the one of biocatalysis in non-conventional media, a pillar of industrial biotechnology. The present article reviews the use of surfactantless microemulsions as effective non-conventional media for enzymatic biotransformations with a focus on oxidases, lipases and their relation to the system's structure.

A novel water-in-oil (W/O) microemulsion based on natural oils, namely extra virgin olive oil (EVOO) and sunflower oil (SO), in the presence of non-ionic surfactants was successfully formulated. The novel microemulsion was used as a carrier for gallic acid (GA) to assure its protection and efficacy upon nasal administration. The work presents evidence that this microemulsion can be used as a nasal formulation for the delivery of polar antioxidants, especially, after incorporation of chitosan (CH) in its aqueous phase. The structure of the system was studied by Small Angle X-ray Scattering (SAXS), Dynamic Light Scattering (DLS) and Electron Paramagnetic Resonance (EPR) spectroscopy techniques. By the addition of CH, the diameter of the microemulsion remained unaltered at 47 nm whereas after the incorporation of GA, micelles with 51 nm diameter were detected. The dynamic properties of the surfactant monolayer were affected by both the incorporation of CH and GA. Moreover, the antioxidant activity of the latter remained unaltered (99 %). RPMI 2650 cell line was used as the in vitro model for cell viability and for GA nasal epithelial transport studies after microemulsion administration. The results suggested that the nasal epithelial permeation of GA was enhanced, 3 h post administration, by the presence of 0.2 % v/v microemulsion in the culture medium. However, the concentration of the transported antioxidant in the presence of CH was higher indicating the polymer’s effect on the transport of the GA. The study revealed that nasal administration of hydrophilic antioxidants could be used as an alternative route besides oral administration.

Monoacylglycerols are increasingly used in several industrial applications as effective and cheap emulsifiers. In the present work monostearin synthesis has been studied, using lipase as a biocatalyst of the esterification reaction of stearic acid with (R,S)-1,2-O-iso-propylidene glycerol (solketal). The lipase from Candida antarctica (CaL B) was immobilized in AOT/isooctane water in oil microemulsions. Optimization of the reaction conditions have shown that the highest production (80% in 30 min) could be achieved at 40 °C, in microemulsions with relatively low water content (wo = 8). Kinetic studies have shown that the esterification reaction of stearic acid with solketal catalyzed by CaL B occurs via the ordered bi–bi mechanism, in which inhibition by the acid was identified. Moreover, at high fixed solketal concentrations a negative cooperativity is pronounced, which means that binding of the alcohol lowers the affinity of the enzyme for binding of the acid. Values of all kinetic parameters have been determined.

Lipases from Rhizomucor miehei (RmL) and Candida antartica (CaL-B) entrapped in surfactant free microemulsion-like ternary systems consisting of n-hexane, short chain alcohols (1-propanol or 2-methyl-2-propanol) and water, keep their catalytic activity at 30 degrees C, catalyzing efficiently the esterification of fatty acids or natural phenolic acids including cinnamic acid derivatives. High conversions (up to 95%) were obtained with both lipases entrapped in various ternary systems. Lipases catalytic efficiency and stability was influenced by the composition of the ternary systems used. Hydroxypropylmethyl cellulose (HPMC) microemulsions-based organogels (MBGs) formulated with various surfactant free microemulsion-like systems were used as a matrix for enzyme immobilization. These lipase-containing MBGs prove to be a novel solid-phase catalyst for use, under mild conditions, in non-polar solvents as well as in solvent free systems. CaL-B immobilized in surfactant free MBGs keep its catalytic activity for a storage period of 8 months, while the corresponding residual activity of immobilized RmL was decreased by 50%. The stability of enzymes in such surfactant free MBGs is higher than that observed in MBGs formulated with surfactant based w/o microemulsions. Lipases-containing surfactant free MBGs were used in seven consecutive batch syntheses of fatty esters with only 10-15% loss of activity. (c) 2005 Elsevier Inc. All rights reserved. Enzyme and Microbial Technology

A series of water-in-oil microemulsion systems formulated without surfactant were used to solubilize lipases from Rhizomucor miehei and Candida antarctica B. The effect of the system's composition on the velocity of enzymic reactions was investigated following a model esterification reaction. The interaction between enzymes and the microemulsion environment was studied by steady state fluorescence spectroscopy. The site of localization of the enzyme within the different microdomains of the dispersed phase was investigated by applying the fluorescence energy transfer technique. To determine the properties of the interface between water and organic solvent of the surfactantless microemulsion systems the Electron Paramagnetic Resonance (EPR) spectroscopic technique was applied. The results indicated that even at low water content, water-rich structures are formed. This was confirmed by conductivity measurements. By the addition of enzyme it was observed that when the aqueous phase of the surfactantless microemulsion systems exceeds 2% (v/v) the enzyme retains its catalytic activity, as it is located within the water pools that protect it from the organic solvent. These confined water phases show a propanol rich interface with hexane and their structure depends on the system's composition. Colloids and Surfaces B: Biointerfaces