Self-assembling of peptide alpha-1 of globin hydrolysates.
1997
Liu X.Q. | Yonekura M. | Tsutsumi M. | Sano Y.
Globin is an edible protein in a large quantity from animal blood. However, globin shows a rather low solubility at neutral pH and little advantage in comparison with other proteins applied to the food industry. To improve its functional properties and to make clear the mechanism of gel formation, the hydrolysis of globin was performed with 0.8 M citric acid. The peptide alpha-1 was obtained by cleavage of the peptide bond between Asp-94 and Pro-95 in the alpha-chain of globin with 0.8 M citric acid. Physicochemical properties and structural characterization of peptide alpha-1 of globin hydrolysates were studied by amino acid sequence analysis, hydrophobic interaction chromatography, and circular dichroism (CD) spectra. The peptide alpha-1 was very highly hydrophilic on hydrophobic chromatography. The concentration dependence of peptide alpha-1 indicated the dissociation and association behaviors analyzed by a light scattering method. Circular dichroism spectra showed that the content of the alpha-helix and beta-sheet structures of peptide alpha-1 were very different from the intact alpha-chain. We have also found that peptide alpha-1 played a role in transformation of aggregates of globin hydrolysates to gel. These results suggest that peptide alpha-1 acts as a cross-linker between the aggregate of globin hydrolysates through the transformation process of gel.
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