STRUCTURAL INVESTIGATION OF THE INTERACTION BETWEEN BOVINE SERUM ALBUMIN AND ACID GELATIN IN WATER - Biochemistry and Biotechnology: Research and Development - page 77

residues, because both, their absorbency at the wavelength of excitation and their quantum
yield of emission, are considerably greater than the respective values for tyrosine and
phenylalanine. We consider the fluorescence quenching of BSA in the presence of gelatin in
terms of local rearrangements of the tryptophan surroundings.
C ONCLUSION
Gelatin molecules are able to form interpolymeric complexes with BSA in water at the
temperatures above the temperature of the conformation transition and BSA/gelatin ratio ~6:1
(mole/mole). Interpolymer interaction leads to collapse gelatin macromolecules due to their
lost of the total negative charge, partial stabilization of the secondary structure (increase the
mean helix content), and stabilization of BSA molecules against thermo aggregation.
At the same time, the thermo aggregation process of BSA molecules passes ahead of their
thermodenaturation process, whereas these two phenomena accompany each other in the
absence of dextran according to Privalov and Potekhin 53 .
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