Submitted to: Pacific Basin Society Chemical International Congress Proceedings
Publication Type: Proceedings
Publication Acceptance Date: 12/20/1995
Publication Date: N/A
Citation: N/A Interpretive Summary:
Technical Abstract: Glycinin, a major storage protein in soybeans, is denatured by moist heat treatment. Secondary structure changes that take place in glycinin upon hydration and heating were studied using infrared spectroscopy. Water alone, from 2.6 to 95%, caused significant broadening in the amide I region and changes in the amide I to amide II maximum absorbance ratio with increased water content. Without heating, these changes were shown to result from changes in the protein-water interactions with no changes in the secondary structure of the glycinin itself. Curve-fitting of deconvoluted infrared spectra gave the same secondary structure at all levels of added water after water contributions were subtracted from the spectra (30% beta, 24% helical, 35% turns and 11% unordered). Secondary structure of heated samples was compared to unheated samples and differential scanning calorimetry results published previously.