Unveiling the critical pH values triggering the unfolding of soy 7S and 11S globulins and enhancing their encapsulation efficiency.

ABSTRACT

The pH-shifting process is an effective encapsulation method, and it is typically performed at extreme alkaline pH, which severely limits the application. In this study, we found that there were critical pH for the unfolding proteins during pH-shifting from 7 to 12, and upon the critical pH, physiochemical characteristics of protein greatly changed, leading to a sharp increase of encapsulation of hydrophobic actives. Firstly, the critical pH for ß-conglycinin (7S) or Glycinin (11S) unfolding was determined by multispectral technology. The critical pH for 7S and 11S were 10.5 and 10.3, respectively. The encapsulation efficiency (EE) obtained by ß-conglycinin-curcumin nanocomposite (7S-Cur) (88.80 %) and Glycinin-curcumin nanocomposite (11S-Cur) (88.38 %) at critical pH was significantly higher than that obtained by pH 7 (7S-Cur = 16.66 % and 11S-Cur = 15.78 %), and both values were close to EE obtained by at 12 (7S-Cur = 95.16 % and 11S-Cur = 94.63 %). The large-scale application of hydrophobic functional compounds will be enhanced by the experimental results.