Abstract
Compatibility is observed in aqueous solutions of serum albumin and pectin (degree of esterification 57%) at pH levels above the isoelectric point of protein. Both the variation in the pH values from 5 to 8 and the increase of ionic strength from 0·1 to 1·0 do not result in phase separation. These facts enable us to conclude that the affinity in this system is of a nonelectrostatic nature. The interaction of serum albumin and pectinate fractions with different degrees of esterification was studied by light scattering. The negative sign of A 24 (the second virial coefficient component of the mixture associated with the interaction between different polymer molecules) means that for any degree of esterification there is affinity between pectin and serum albumin. Information concerning excess thermodynamic functions was obtained from the temperature dependence of light scattering. Mixing microcalorimetry was used for precise measurement of enthalpy. The experimental results indicate that thermodynamic compatibility of serum albumin and pectin is controlled by increase of mixing entropy, which mainly stems from dehydration of biopolymer macromolecules during contact formation.
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