Abstract
Four gelatin types (A, B, C and AB), two different samples of each, were subjected to temperature treatments with the incubation temperature, incubation time, gelatin concentration and solvent (type and concentration of salt ions and pH) as variables. Degradation was studied by means of fast protein liquid chromatography and sodium dodecylsulphate polyacrylamide gel electrophoresis. All the variables tested seemed to be critical. Addition of a protease inhibitor cocktail confirmed that the observed degradation was not due to the action of proteases. Fluorescence measurements indicated that during the temperature treatment pentosidine and pyridinoline cross-links can be broken, while the cleavage of peptide bonds was verified by ninhydrin tests and N-terminal amino-acid analyses with phenyl isothiocyanate.
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