This project was supported by the Iowa Agriculture & Home Economics Experiment Station, projects 2433 and 2164 (NC-136) and the Iowa Soybean Promotion Board and published as Journal J-13621.
Temperature Effect on Binding of Volatile Flavor Compounds to Soy Protein in Aqueous Model Systems
Version of Record online: 25 AUG 2006
Journal of Food Science
Volume 56, Issue 3, pages 802–806, May 1991
How to Cite
O'KEEFE, S. F., RESURRECCION, A. P., WILSON, L. A. and MURPHY, P. A. (1991), Temperature Effect on Binding of Volatile Flavor Compounds to Soy Protein in Aqueous Model Systems. Journal of Food Science, 56: 802–806. doi: 10.1111/j.1365-2621.1991.tb05386.x
- Issue online: 25 AUG 2006
- Version of Record online: 25 AUG 2006
- Ms received 7/23/90; revised 9/24/90; accepted 11/15/90.
The thermodynamics of binding was determined for soybean glycinin and β-conglycinin and flavor ligands butanal, pentanal, hexanal, octanal, 2- and 3-hexanone, 2- and 5-nonanone, hexanol, and hexane. Hexane had affinity for these proteins only at 5oC. Affinities of binding for all flavor ligands were greater for glycinin than β-conglycinin. Affinity for aldehydes increased with increasing chain length for glycinin, but remained constant for β-conglycinin. ΔGo, ΔHo, and ΔSo for binding were determined. ΔGo was negative for all ligands and ranged from −1.74 to −4.16 Kcal/mol. All enthalpies of binding were positive except butanal and hexanol. Change in free energy of binding per CH2 in homologous aldehydes was greater for glycinin than β-conglycinin.