S. Petruccelli et Mc. Anon, PARTIAL REDUCTION OF SOY PROTEIN ISOLATE DISULFIDE BONDS, Journal of agricultural and food chemistry, 43(8), 1995, pp. 2001-2006
Partial reduction of disulfide bonds of soy protein isolates was follo
wed electrophoretically. Isolates treated with Na2SO3 under different
conditions showed disappearance of high molecular weight aggregates. A
cidic 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 o
f a catalyst (Cu) and oxygen showed a similar effect in the sulfitolys
is of soy proteins with Na2SO3. 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 co
mponents other than AB-11S subunits were reduced when Na2SO3 was used
in the presence of Cu and/or oxygen.