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Abstract
When the 11S globulin, one of the major storage proteins in soybean seeds ( Glycine max), was heated at 0·5 ionic strength, the denaturation temperature was biologically estimated to be about 10 degrees higher than that at 0·1 ionic strength. The results also coincided well with those obtained by differential scanning calorimetry. The heat denaturation temperatures of the protein obtained by differential scanning calorimetry were estimated to be 78·1°C and 89·6°C at 0·1 and 0·5 ionic strength respectively. The enthalpies of heat denaturation were 2·0 cal/g and 3·2cal/g at 0·1 and 0·5 ionic strength, respectively. Correlation was not observed between the heat stability at high ionic strength and the content of the ordered secondary structure or a dissociation-association reaction of the protein with change of ionic strength. However, increase of the hydrophobic region at high ionic strength indicated the possibility of stabilisation of the quaternary structure of the 11S globulin by hydrophobic bonding during heat denaturation.
Published Version
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