Polar hydrophilic solvents

Aqueous solutions are not suitable solvents for esterifications and transesterifications, and these reactions are carried out in organic solvents of low polarity [9-12]. However, enzymes are surrounded by a hydration shell or bound water that is required for the retention of structure and catalytic activity [13]. Polar hydrophilic solvents such as DMF, DMSO, acetone, and alcohols (log P<0, where P is the partition coefficient between octanol and water) are incompatible and lead to rapid denaturation. Common solvents for esterifications and transesterifications include alkanes (hexane/log P=3.5), aromatics (toluene/2.5, benzene/2), haloalkanes (CHCI3/2, CH2CI2/I.4), and ethers (diisopropyl ether/1.9, terf-butylmethyl ether/ 0.94, diethyl ether/0.85). Exceptionally stable enzymes such as Candida antarctica lipase B (CAL-B) have been used in more polar solvents (tetrahydrofuran/0.49, acetonitrile/—0.33). Room-temperature ionic liquids [14—17] and supercritical fluids [18] are also good media for a wide range of biotransformations. 

It was early discovered that enzyme activity in organic solvents depends very much on the nature of the solvent. It was realized that the polarity or hydrophobicity of the solvent had a large influence, with non-polar hydrophobic solvents often providing higher reaction rates than more polar, hydrophilic solvents. When the kinetics of enzymatic reactions is studied, it is often found that Km values in organic solvents are much higher than those in water for the corresponding... 

Loop regions exposed to solvent are rich in charged and polar hydrophilic residues. This has been used in several prediction schemes, and it has proved possible to predict loop regions from an amino acid sequence with a higher degree of confidence than a helices or p strands, which is ironic since the loops have irregular structures. 

The term "hydrophilic force", literally meaning "love of water" force, was introduced as a complement to "hydrophobic force". Hydrophilic forces are equivalent to polar forces, and polar solvents that interact strongly with water are called hydrophilic solvents. 

Of particular interest when considering ionizable compounds is the difference of lipophilicity between the neutral species and one of its ionic forms, because ionization dramatically alters intramolecular interactions (such as electronic conjugation, internal ionic and hydrogen bonds, polarity, hydrophilic folding, and shielding). In a given solvent system, diff (log is approximately constant for compounds with similar chemical... 

A practical enzymatic procedure using alcalase as biocatalyst has been developed for the synthesis of hydrophilic peptides.Alcalase is an industrial alkaline protease from Bacillus licheniformis produced by Novozymes that has been used as a detergent and for silk degumming. The major enzyme component of alcalase is the serine protease subtilisin Carlsberg, which is one of the fully characterized bacterial proteases. Alcalase has better stability and activity in polar organic solvents, such as alcohols, acetonitrile, dimethylformamide, etc., than other proteases. In addition, alcalase has wide specificity and both l- and o-amino acids that are accepted as nucleophiles at the p-1 subsite. Therefore, alcalase is a suitable biocatalyst to catalyse peptide bond formation in organic solvents under kinetic control without any racemization of the amino acids (Scheme 5.1). 

PAMAM dendrimers are large (G4 is 4.5 nm in diameter) and have a hydrophilic interior and exterior accordingly, they are soluble in many convenient solvents (water, alcohols, and some polar organic solvents). Importantly, the interior void spaces are large enough to accommodate nanoscopic guests, such as metal clusters, and are sufficiently monodispersed in size so as to ensure fairly uniform particle size and shape. As we will show later, the space between the ter-... 

Water-in-oil concentrated emulsions have also been utilised in the preparation of polymer latexes, from hydrophilic, water-soluble monomers. Kim and Ruckenstein [178] reported the preparation of polyacrylamide particles from a HIPE of aqueous acrylamide solution in a non-polar organic solvent, such as decane, stabilised by sorbitan monooleate (Span 80). The stability of the emulsion decreased when the weight fraction of acrylamide in the aqueous phase exceeded 0.2, since acrylamide is more hydrophobic than water. Another point of note is that the molecular weights obtained were lower compared to solution polymerisation of acrylamide. This was probably due to a degree of termination by chain transfer from the tertiary hydroxyl groups on the surfactant head group. 

The biochemical structure of a membrane is that of a lipid bilayer composed of phospho- and sphingolipids, as well as cholesterol. These lipids are amphipathic in nature, that is, they each have a polar and a nonpolar end. In water the nonpolar (hydrophobic, lipophilic) ends will seek to avoid the polar solvent and aggregate into a bilayer with the polar (hydrophilic, lipophobic) ends oriented towards the outside of the bilayer. As this structure extends in all directions the exposed nonpolar regions will close up and form a sphere (or ellipsoid) with water trapped inside and excluded outside. See Figures 2a and 2b. 

A graphic representation of a three-dimensional model of the protein, cytochrome c. Amino acids with nonpolar, hydrophobic side chains (color) are found in the interior of the molecule, where they interact with one another. Polar, hydrophilic amino acid side chains (gray) are on the exterior of the molecule, where they interact with the polar aqueous solvent. (Illustration copyright by Irving Geis. Reprinted by permission.)... 

Surfactants Surfactants are molecules made up of a polar hydrophilic head group and a hydrophobic hydrocarbon tail, which leads these molecules to favor as being at the interface between two phases.31 Membranes that were previously used, such as solvent-cast cellulose acetate72 or dip-coated polyurethane membranes,73 can be modified by surfactants to decrease biofouling. Lindner et al. showed that membranes with lower surfactant plasticizer ratios exhibited lower anion interference and better biocompatibility.74... 

The major problem associated with the enzymatic acylation of sucrose is the incompatibility of the two reactants sucrose and a fatty acid ester. Sucrose is hydrophilic and readily soluble in water or polar aprotic solvents such as pyridine and dimethylformamide. The former is not a feasible solvent for (trans)esterifi-cations, for obvious thermodynamic reasons, and the latter are not suitable for the manufacture of food-grade products. The selective acylation of sucrose, as a suspension in refluxing tert-butanol, catalyzed by C. antarctica lipase B, afforded a 1 1 mixture of the 6 and 6 sucrose monoesters (Fig. 8.39) [208]. Unfortunately, the rate was too low (35% conversion in 7 days) to be commercially useful. 

Attempts have been made to correlate the influence of solvents on enzyme activity, stability, and selectivity with physicochemical solvent characteristics such as relative permittivity, dipole moment, water miscibility, and hydrophobicity, as well as empirieal parameters of solvent polarity. However, no rationale of general validity has been found, except the simple rule that nonpolar hydrophobic solvents are generally better than polar hydrophilic ones. The best correlations are often obtained with the logarithm of the 1-octanol/water partition coefficient, Ig Pq/wj a quantitative measure of the solvent s hydrophobicity cf. Section 7.2). 

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