Partial reduction of soy protein isolate disulfide bonds

SILVANA PETRUCCELLI; AÑÓN, M. C.

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

American Chemical Society

Lugar: Davis; Año: 1995 vol. 53 p. 2001 - 2006

0021-8561

Partial reduction of disulfide bonds of soy protein isolates was followed electrophoretically. Isolates treated with Na2S03 under different conditions showed disappearance of high molecular weight aggregates. Acidic and basic 11s polypeptides and some whey proteins that remain in the isolates were also affected; reduction of the AB-11s subunit was very limited. The sulfitolysis method was also studied. The addition of a catalyst (CUI and oxygen showed a similar effect in the sulfitolysis of soy proteins with Na2S03. To achieve complete sulfitolysis, the presence of a denaturing and an oxidizing agent were needed. Mainly AB subunits of glycinin were reduced when urea was used, while mostly components other than AB-11s subunits were reduced when Na2S03 was used in the presence of Cu andor oxygen.