Abstract
This work investigated and compared the structural and emulsifying properties of peanut globulin fractions (conarachin and arachin) after ultrasonication (US) and pH2.5-shifting treatments, singly and in combination. Results showed that pH2.5-shifting was more effective in degrading peanut protein subunits and unfolding their structures than US treatment. Conarachin tended to aggregate during US and pH2.5-shifting treatments possibly due to higher free sulfhydryl content, while high molecular weight arachin tended to disaggregate during these treatments. pH2.5-shifting or US+pH2.5-shifting treatments significantly increased the surface hydrophobicity of conarachin (from 72 to 314) and arachin (from 336 to 888), which may be responsible for the enhancement of protein emulsifying activity. All treatments significantly improved the physical stability of arachin-stabilized emulsions with higher absolute potentials but lowered that of conarachin-stabilized emulsions. However, pH2.5-shifting or US+pH2.5-shifting treatments could improve the stability of conarachin-stabilized emulsions in the presence of salts.