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Physics Reports vol.72

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Ch002 46 PHENOLIC COMPOUNDS IN FOOD AND THEIR EFFECTS ON HEALTH I finally 'anchored' by hydrogen bonding, the emphasis is now more clearly upon the whole process of molecular recognition beginning with the initially solvated species. From this point a whole range of factors may then influence the recognition process and the strength of the intermolecular bonds which are formed One might be excused if,froma cursory inspection of a molecular model of a typical polyphenol, one assumed that the phenolic hydroxyl groups, which dominate the appearance of the exterior surface of the polyphenol, also dominated its complexation behaviour.

Alternative approaches to these and related problems have been utilised in the authors' laboratory. Particular questions which have been addressed include :(i) ( ii ) ( iii ) ( iv ) (ν) How is the structure of a polyphenol related to its capacity to bind to a given protein ? Can evidence be obtained to demonstrate the presence of soluble polyphenol - protein complexes ? Is there a direct relationship between the ability of a polyphenol to reversibly complex with a given protein ( K, Figure 1 ), and its ability to precipitate that protein ?

Caseins. Similar observations in type may be made with calcium and the caseins ( 42 ). Caseins are a major group of secretory proteins synthesised during mammalian lactation and are stored and secreted as stable calcium phosphate complexes. These occur in milk in more or less spherical micelle particles. The caseins are phosphoproteins and fall into two groups which differ in their sensitvity to precipitation by calcium ions. In the cow these comprise the calcium insensitive κ casein family and the calcium sensitive caseins - ocsi, otS2 and β caseins.

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