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High-resolution carbon-13 nuclear magnetic resonance study of the soybean 7S storage protein fraction in solution

, : High-resolution carbon-13 nuclear magnetic resonance study of the soybean 7S storage protein fraction in solution. Journal of agricultural and food chemistry 38(12): 2126-2132

The molecular structure and dynamics of soybean 7S storage proteins were investigated by high-resolution 13C NMR at high fields (7.05 and 11.75 T). The spectrum of the alkali-denatured proteins (pH 12.0) is well-resolved, and tentative assignments of 53 peaks are given. At pH 12.0 and 12 mM ionic strength the proteins dissociate into partially unfolded subunits that exhibit fast local motion (10(-9)-10(-10) s), while they maintain a relatively immobile hydrophobic core. The spectra of "native", multisubunit proteins consist of broad peaks as a result of the slower protein tumbling in solution and the expected chemical shift nonequivalence. There is evidence that Phe residues are in the hydrophobic subunit core, whereas Tyr residues are found at the subunits' interface. No major spectral differences were observed between pH 7.6 and 10.3 (at 0.5 M ionic strength, where proteins exist as trimers) or between 13 mM ionic strength and 0.5 M NaCl (at pH 10.2, where a trimer-hexamer interconversion occurs). Potential applications of these results, and of the 13C NMR techniques, in general, include quality control of soy protein isolates in food engineering and the analysis of complex foods that include soy protein ingredients.


DOI: 10.1021/jf00102a005

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