Thermal Aggregation of Soy Protein Isolates

PETRUCCELLI, S; AÑÓN, M.C.

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

AMER CHEMICAL SOC

Año: 1995 vol. 43 p. 3035 - 3041

0021-8561

Thermal behavior of soy protein isolates under different conditions of temperature, time, pH, protein concentration, and presence of reducing agents was studied. Thermal treatments above 85 "C showed a decrease in concentration of the AB-11s subunit and of the two protein species of 20 and 29 kDa, and a gradual increase in the concentration of the A and B polypeptides of glycinin. None of the thermal treatments tested led to modifications of the relative proportions either of the high molecular weight aggregates (100-200 kDa) observed in the electrophoretic profiles or of the a' and a subunits of P-conglycinin; Increasing the pH to 9 or 10 and increasing the protein isolate concentration enhanced AB-11s aggregation during the thermal treatment. Either the presence of Na2S03 or the pH 9- 10 favored the P-P-conglycinin/B-glycinin aggregation. This interaction requires an increase of SH groups. Initially the P-P-conglycinin/B-glycinin aggregates were stabilized by hydrophobic interactions and later by SS bonds.85 "C showed a decrease in concentration of the AB-11s subunit and of the two protein species of 20 and 29 kDa, and a gradual increase in the concentration of the A and B polypeptides of glycinin. None of the thermal treatments tested led to modifications of the relative proportions either of the high molecular weight aggregates (100-200 kDa) observed in the electrophoretic profiles or of the a' and a subunits of P-conglycinin; Increasing the pH to 9 or 10 and increasing the protein isolate concentration enhanced AB-11s aggregation during the thermal treatment. Either the presence of Na2S03 or the pH 9- 10 favored the P-P-conglycinin/B-glycinin aggregation. This interaction requires an increase of SH groups. Initially the P-P-conglycinin/B-glycinin aggregates were stabilized by hydrophobic interactions and later by SS bonds.the concentration of the A and B polypeptides of glycinin. None of the thermal treatments tested led to modifications of the relative proportions either of the high molecular weight aggregates (100-200 kDa) observed in the electrophoretic profiles or of the a' and a subunits of P-conglycinin; Increasing the pH to 9 or 10 and increasing the protein isolate concentration enhanced AB-11s aggregation during the thermal treatment. Either the presence of Na2S03 or the pH 9- 10 favored the P-P-conglycinin/B-glycinin aggregation. This interaction requires an increase of SH groups. Initially the P-P-conglycinin/B-glycinin aggregates were stabilized by hydrophobic interactions and later by SS bonds.a' and a subunits of P-conglycinin; Increasing the pH to 9 or 10 and increasing the protein isolate concentration enhanced AB-11s aggregation during the thermal treatment. Either the presence of Na2S03 or the pH 9- 10 favored the P-P-conglycinin/B-glycinin aggregation. This interaction requires an increase of SH groups. Initially the P-P-conglycinin/B-glycinin aggregates were stabilized by hydrophobic interactions and later by SS bonds.AB-11s aggregation during the thermal treatment. Either the presence of Na2S03 or the pH 9- 10 favored the P-P-conglycinin/B-glycinin aggregation. This interaction requires an increase of SH groups. Initially the P-P-conglycinin/B-glycinin aggregates were stabilized by hydrophobic interactions and later by SS bonds.P-P-conglycinin/B-glycinin aggregation. This interaction requires an increase of SH groups. Initially the P-P-conglycinin/B-glycinin aggregates were stabilized by hydrophobic interactions and later by SS bonds.SS bonds.