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Food Lipids: Chemistry, Nutrition, and Biotechnology

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pensations in that enthalpy lost by lipids undergoing transition is absorbed by membrane<br />

proteins as they partition into the more fluid phase of the bilayer [14].<br />

For complex mixtures of lipids found in biological membranes, at temperatures<br />

above the phase transition, all component lipids are liquid crystalline, exhibiting<br />

characteristics consistent with complete mixing of the various lipids. At temperatures<br />

below the phase transition of the phospholipid with the highest melting temperature,<br />

separation of the component into crystalline domains (lateral phase separation) can<br />

occur. This ability of individual lipid components to adopt gel or liquid crystalline<br />

arrangements has led to the suggestion that particular lipids in a biological membrane<br />

may become segregated into a local gel state. This segregation could affect protein<br />

function by restricting protein mobility in the bilayer matrix, or it could provide<br />

packing defects, resulting in permeability changes. Exposure of plant food tissues to<br />

refrigerator temperatures could thus induce localized membrane phase transitions,<br />

upset metabolic activity, <strong>and</strong> create an environment that serves to reduce the quality<br />

of the product [15].<br />

Several compositional factors play a role in determining transition temperatures<br />

of membranes. The longer the chain length in a phospholipid class, the higher the<br />

transition temperature. Similarly, cation binding to PS membranes decreases the<br />

phase transition temperature. However, the presence of cis double bonds on the<br />

phospholipid fatty acids inhibits hydrocarbon chain packing in the gel state <strong>and</strong><br />

causes the phase transition to occur at a lower temperature. On the other h<strong>and</strong>, the<br />

presence of the free fatty acid, oleic acid, had negligible effects on the bilayer phase<br />

transition, whereas the free fatty acid, palmitic acid, increased the bilayer phase<br />

transition temperature [16]. Differential effects on bilayer properties were also seen<br />

by the incorporation of cholesterol, <strong>and</strong> these effects were dependent on the cholesterol<br />

concentration [17]. In small amounts (�3 mol %), a softening of the bilayers<br />

in the transition region occurred. However, higher cholesterol concentrations led to<br />

a rigidification of the bilayer that was characterized as a liquid-ordered phase. This<br />

phase is liquid in the sense that the molecules diffuse laterally as in a fluid, but at<br />

the same time the lipid-acyl chains have a high degree of conformational order.<br />

D. Membrane Lipid–Protein Interactions<br />

Complete functioning of a biomembrane is controlled by both the protein <strong>and</strong> the<br />

lipid, mainly phospholipid, components. In a bilayer membrane that contains a heterogeneous<br />

distribution of both peripheral <strong>and</strong> integral proteins, there will be a certain<br />

proportion of the phospholipids interacting with the protein component to give<br />

the membrane its integrity at both the structural <strong>and</strong> the functional level. Thus, the<br />

proportion of phospholipids in the bilayer interacting with protein at any one time<br />

is dictated by protein density, protein type, protein size, <strong>and</strong> aggregation state of the<br />

proteins.<br />

The major structural element of the transmembrane part of many integral proteins<br />

is the �-helix bundle <strong>and</strong> the disposition <strong>and</strong> packing of such helices determine<br />

the degree of protein–lipid interactions. A single � helix passing through a bilayer<br />

membrane has a diameter of about 0.8–1 nm, depending on side chain extension,<br />

which is similar to the long dimension of the cross-section of a diacyl phospholipid<br />

(�0.9–1.0 nm) [18]. In the absence of any significant lateral restriction of such an<br />

individual peptide helix, the lateral <strong>and</strong> rotational motion of the peptide will be<br />

Copyright 2002 by Marcel Dekker, Inc. All Rights Reserved.

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