Heat denaturation of soy glycinin: influence of pH and ionic strength on molecular structure.
The 7S/11S glycinin equilibrium as found in Lakemond et al. (J. Agric. Food Chem. 2000, 48, xxxx-xxxx) at ambient temperatures influences heat denaturation. It is found that the 7S form of glycinin denatures at a lower temperature than the 11S form, as demonstrated by a combination of calorimetric (DSC) and circular dichroism (CD) experiments. At pH 7.6, at which glycinin is mainly present in the 11S form, the disulfide bridge linking the acidic and the basic polypeptides is broken during heat denaturation. At pH 3.8, at which glycinin has dissociated partly into the 7S form, and at pH 5.2 this disruption does not take place, as demonstrated by solubility and gel electrophoretic experiments. A larger exposure of the acidic polypeptides (Lakemond et al., 2000) possibly correlates with a higher endothermic transition temperature and with the appearance of an exothermic transition as observed with DSC. Denaturation/aggregation (studied by DSC) and changes in secondary structure (studied by far-UV CD) take place simultaneously. Generally, changes in tertiary structure (studied by near-UV CD) occur at lower temperatures than changes in secondary structure.
Lakemond
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CM
Centre for Protein Technology TNO-WU, Wageningen, The Netherlands.
de Jongh
H H
HH
Hessing
M
M
Gruppen
H
H
Voragen
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AG
D002942:Circular Dichroism; D005916:Globulins / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D012995:Solubility; D030262:Soybean Proteins; D013025:Glycine max; D013816:Thermodynamics
D005916:Globulins; D010940:Plant Proteins; D030262:Soybean Proteins; C011474:glycinin