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Home » Biology Homework Help » Biotechnology » Biphasic Systems
Biphasic Systems
Enzymatic reactions in a biphasic liquid system are advantageous for the following reasons: (i) ease in separation and recovery of products, (ii) higher yields due to product and enzyme lying in separate phases, (iii) greater solubility of the substrate in the second phase, e.g. an organic solvent, (iv) instability of the product in aqueous phase but not in the organic phase, and (v) favourable change in the equilibrium constants of reactions leading to higher product yields.

A biphasic liquid system consists of two immiscible liquids in which the enzyme is able to function and remains fairly stable. The biphasic systems may be of two types:
   
Aqueous two-phase systems

In such systems both the phases are aqueous but they contain different polymers which do not mix together. The most extensively studied system of this type is produced by the polymers PEG (10% w/v of PEG 4000) and dextran (2% w/v of dextran T 500). When PEG and dextran are mixed in water, they separate into two layers (phases): (i) the lower, more hydrophilic and denser phase formed by dextran, and (ii) less dense, more hydrophobic, upper phase containing PEG. Phases are formed when polymers are used in concentrations higher than their limiting concentrations, which depend on their molecular weight, pH temperature and ionic strength. The polymers have stabilizing effect on most proteins. Such systems facilitate a variety of separations, e.g. separation of enzymes from cell materials in their mass production, in a matter of few minutes.
   
Aqueous-Organic biphasic systems

In these systems, enzyme molecules are suspended within an organic solvent (the organic phase) and the aqueous phase is represented by the thin layer of water surrounding each enzyme molecule. The small amounts of water (50-500 molecules/enzyme molecule) are essential for stability and integrity of hydrophilic enzymes; hydrophobic enzymes like lipases (enzymes associated with lipids and membranes) may remain active even with fewer water molecules. Thus the enzymes in non-aqueous solvents are generally in an almost anaqueous state; this greatly enhances their thermostability. However, if even this small amount of water associated with the enzyme molecules is removed, the enzymes are inactivated. In general, solvents of lower polarity, i.e. greater hydrophobicity are better in maintaining enzyme stability.



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