Hydrophobic organic substrates

MOBILISATION OF HYDROPHOBIC ORGANIC SUBSTRATES USING BIOSURFACTANTS... 

Microbes were frequently found to synthesise surface-active molecules in order to mobilise hydrophobic organic substrates. These biosurfactants, which are either excreted by the producing organisms or remain bound to their cell surfaces, are composed of a hydrophilic part making them soluble in water and a lipophilic part making them accumulate at interfaces. With respect to their physical effects, one can distinguish two types of biosurfactants firstly, molecules that drastically reduce the surface and interfacial tensions of gas-liquid, liquid-liquid and liquid-solid systems, and, secondly, compounds that stabilise emulsions of nonaqueous phase liquids in water, often also referred to as bioemulsifiers. The former molecules are typically low-molar-mass... 

Equilibrium constants for the binding between substrates and micelles — Reaction (G) — generally range from 103 to 106 for hydrophobic organic substrates. Furthermore, they are expected to increase as the hydrophobic character of the substrate increases. Figure 8.10b shows that this effect sometimes overshoots optimum solubilization. The figure shows, on a... 

Another type of structurally ill-defined emulsion between water and organic compounds can be applied as an efficient reaction medium for reactions between hydrophilic inorganic salts and hydrophobic organic substrates. So-called microemulsions are particularly useful in the case where the isolation of the reaction products is not necessary. 

Hydrophilic anions will stay in the outer, water-rich regions of micelles and the more hydrophobic organic substrates may be located more deeply in the micelle. These effects, and those due to the preferred orientation of substrates in the micelle, do not seem to be of major importance in determining k /k, because values are not very different for reactions of substrates which have the same reactive groups but different hydrophobici-ties. This conclusion is illustrated by comparing values of k lk, for reactions of OH with 4-nitrophenyl acetate and octanoate or of CN with a series of N-alkylpyridinium ions (Tables 3 and 4). Despite large differences in hydro-phobicities, as shown by variations in K there is little change in (Il is... 

The same group also reported an amphiphiHc PS-PEG resin-supported mthe-nium complex, which could catalyze the Kharasch reaction in water under heterogeneous conditions without any radical initiators (Scheme 8.29) [65]. Owing to the self-concentration of hydrophobic organic substrates inside the polymer matrix in water, it was claimed that the catalytic efficiency of the PS-PEG Ru in water was comparable to the most efficient homogeneous Ru catalysis reported thus far. 

Figure 17.3 Anatomy of a redox enzyme representation of the X-ray crystallographic structure of Trametes versicolor laccase III (PDB file IKYA) [Bertrand et al., 2002]. The protein is represented in green lines and the Cu atoms are shown as gold spheres. Sugar moieties attached to the surface of the protein are shown in red. A molecule of 2,5-xyhdine that co-crystallized with the protein (shown in stick form in elemental colors) is thought to occupy the broad-specificity hydrophobic binding pocket where organic substrates ate oxidized by the enzyme. Electrons from substrate oxidation are passed to the mononuclear blue Cu center and then to the trinuclear Cu active site where O2 is reduced to H2O. (See color insert.)...

The conclusions of the preceding discussion can be briefly summarized as follows. The formation of inclusion complexes in both the crystalline state as well as in solution has been convincingly demonstrated by spectral and kinetic techniques. Whereas the crystalline complexes are seldom stoichiometric, the solution complexes are usually formed in a 1 1 ratio. Although the geometries within the inclusion complexes cannot be accurately defined, it is reasonable to assume that an organic substrate is included in such a way to allow maximum contact of the hydrophobic portion of the substrate with the apolar cycloamylose cavity. The hydrophilic portion of the substrate, on the other hand, probably remains near the surface of the complex to allow maximum contact with the solvent and the cycloamylose hydroxyl groups. The implications of inclusion complex formation for specificity and catalysis will be elucidated in subsequent sections of this article. 

This discussion has emphasized the idea that the interaction of the cyclo-amyloses with organic substrates is more favorable than the interaction of the individual molecules with water. In the sense that the driving force for the inclusion process appears as a favorable enthalpy of association, this may be thought of as an atypical hydrophobic interaction. 

Micelles forming above the c.m.c. incorporate hydrophobic molecules in addition to those dissolved in the aqueous phase, which results in apparently increased aqueous concentrations. It has to be noted, however, that a micelle-solubilised chemical is not truly water-dissolved, and, as a consequence, is differently bioavailable than a water-dissolved chemical. The bioavailability of hydrophobic organic compounds was, for instance, reduced by the addition of surfactant micelles when no excess separate phase compound was present and water-dissolved molecules became solubilised by the micelles [69], In these experiments, bacterial uptake rates were a function of the truly water-dissolved substrate concentration. It seems therefore that micellar solubilisation increases bioavailability only when it transfers additional separate phase substrate into the aqueous phase, e.g. by increasing the rates of desorption or dissolution, and when micelle-solubilised substrate is efficiently transferred to the microorganisms. Theoretically, this transfer can occur exclusively via the water phase, involving release of substrate molecules from micelles, molecular diffusion through the aqueous phase and microbial uptake of water-dissolved molecules. This was obviously the case, when bacterial uptake rates of naphthalene and phenanthrene responded directly to micelle-mediated lowered truly water-dissolved concentrations of these chemicals [69]. These authors concluded from their experiments that micellar naphthalene and phenanthrene had to leave the micellar phase and diffuse through the water phase to become... 

Li, et al. reported ethyl-bridged PMOs with Pd(ll) complexed to 3-aminopropyl-Itrimethoxysilane grafted onto the mesoporous walls to be an efficient catalysts for Barbier reaction of benzaldehyde and allyl bromide (Figure 16) [74]. Use of water as the reaction medium combined with the presence of ethyl moiety in the framework (which increased hydrophobicity of the pores) enhanced diffusion of the organic substrates. As can be seen in Table 3 the PMO material showed superior catalytic efficiency compared to grafted SBA-15 and MCM-41 materials with values comparable to homogeneous trials. 

The lipase-catalyzed resolutions usually are performed with racemic secondary alcohols in the presence of an acyl donor in hydrophobic organic solvents such as toluene and tert-butyl methyl ether (Scheme 1.3). In case the enzyme is highly enantioselective E = 200 or greater), the resolution reaction in general is stopped at nearly 50% conversion to obtain both unreacted enantiomers and acylated enantiomers in enantiomerically enriched forms. With a moderately enantioselective enzyme E = 20-50), the reaction carries to well over 50% conversion to get unreacted enantiomer of high optical purity at the cost of acylated enantiomer of lower optical purity. The enantioselectivity of lipase is largely dependent on the structure of substrate as formulated by Kazlauskas [6] most lipases show... 

BMIM]BF4 was applied to a Suzuki reaction. The active catalyst was a trico-ordinated [Pd(PPh3)2(Ar)][X] complex that formed after oxidative addition of aryl halide to [Pd(0)(PPh3)4] 211). The hydrophobic ionic liquid does not compete with the unsaturated organic substrate for the electrophilic active metal center. 

Thus, the possibility of adsorption is of primary importance. Adsorption may originate either from chelating properties of the organic substrate toward surface metal species or, because of the low hydrophobicity of the metal oxide surface, from the expulsion of the organic molecules from the solution for entropy reasons. Because there is depletion of substrate at the catalyst surface when degradation takes place, migration from the solution is assisted by a concentration difference in the two environments. 

The entire iron-porphyrin-protein complex is called a cytochrome and such proteins are important electron-transfer components of cells. Generally, access to the macromolecular region in which the oxidation reactions occur is via a hydrophobic channel through the protein (Mueller et al., 1995). As a result, organic substrates are transferred from aqueous solution into the enzyme s active site primarily due to their hydrophobicity and are limited by their size. This important feature seems very appropriate hydrophobic molecules are selected to associate with this enzyme, and these are precisely the ones that are most difficult for organisms to avoid accumulating from a surrounding aquatic environment. 

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