Surface Tension proteins,

Surface tension Protein adsorption Often high volumes are required... 

Key words Surface tension, protein-amphiphile interaction... 

The primary site of action is postulated to be the Hpid matrix of cell membranes. The Hpid properties which are said to be altered vary from theory to theory and include enhancing membrane fluidity volume expansion melting of gel phases increasing membrane thickness, surface tension, and lateral surface pressure and encouraging the formation of polar dislocations (10,11). Most theories postulate that changes in the Hpids influence the activities of cmcial membrane proteins such as ion channels. The Hpid theories suffer from an important drawback at clinically used concentrations, the effects of inhalational anesthetics on Hpid bilayers are very small and essentially undetectable (6,12,13). 

In the absence of specific interactions of the receptor - ligand type the change in the Helmholtz free energy (AFadj due to the process of adsorption is AFads = yps - ypi - Ysi, where Yps, YPi and ys, are the protein-solid, protein-liquid and solid-liquid interfacial tensions, respectively [5], It is apparent from this equation that the free energy of adsorption of a protein onto a surface should depend not only of the surface tension of the adhering protein molecules and the substrate material but also on the surface tension of the suspending liquid. Two different situations are possible. 

For Yiv > YPv> where y v and Ypv are the surface tensions of liquid and protein, respectively, AFads increases with increasing ysv, predicting decreasing polymer adsorption. An example of this is phosphate buffer saline where y]v = 72.9 mJ/m2 and Ypv is usually between 65 and 70mJ/m2 for most proteins [5]. Therefore, supports for gel-permeation and affinity chromatography should be as hydrophilic as possible in order to minimize undesirable adsorption effects. 

In a gas and liquid system, when gas is introduced into a culture medium, bubbles are formed. The bubbles rise rapidly through the medium and dispersion of the bubbles occurs at surface, forming froth. The froth collapses by coalescence, but in most cases the fermentation broth is viscous so this coalescence may be reduced to form stable froth. Any compounds in the broth, such as proteins, that reduce the surface tension may influence foam formation. The stability of preventing bubbles coalescing depends on the film elasticity, which is increased by the presence of peptides, proteins and soaps. On the other hand, the presence of alcohols and fatty acids will make the foam unstable. 

Another important factor is that the surface film must not coalesce readily. Adams (1) states that more important than low surface tension for the stability of a foam is that the solution have a surface tension which is easily and quickly variable. Animal and vegetable proteins added to a solution in the proper amounts, aided by stabilizers, fulfill these needs in the food field. 

Secondly, a stable icing foam requires a low surface tension. Consider the case of egg whites in a beater. With slight whipping, entrapped air bubbles are large and the whites appear foamy, yet transparent and runny. With longer whipping the whites become less transparent, white, and more solid. Thus, because of the low surface tension inherent in the egg protein in solution, more and more air may be incorporated and held in place by the colloidal protein which forms a film around each air cell. 

Retention in HIC can be described in terms of the solvophobic theory, in which the change in free energy on protein binding to the stationary phase with the salt concentration in the mobile phase is determined mainly by the contact surface area between the protein and stationary phase and the nature of the salt as measured by its propensity to increase the surface tension of aqueous solutions [331,333-338]. In simple terms the solvopbobic theory predicts that the log u ithn of the capacity factor should be linearly dependent on the surface tension of the mobile phase, which in turn, is a llne2u function of the salt concentration. At sufficiently high salt concentration the electrostatic contribution to retention can be considered constant, and in the absence of specific salt-protein interactions, log k should depend linearly on salt concentration as described by equation (4.21)... 

I Sugars (sucrose, glucose, mannose) Surface tension increase Inert Good stabilizers of globular proteins and assembled organelles... 

Some amino acids (glycine, alanine, glutamic, and aspartic acids) Surface tension increase Weak binding Stabilizers of globular proteins... 

Salting-out salts (Na2S04, NaCl, MgS04) Surface tension increase Weak binding Stabilize globular proteins and precipitants of native and denatured proteins... 

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