THERMAL AGGREGATION OF SOY PROTEIN ISOLATES

Citation
S. Petruccelli et Mc. Anon, THERMAL AGGREGATION OF SOY PROTEIN ISOLATES, Journal of agricultural and food chemistry, 43(12), 1995, pp. 3035-3041
Citations number
24
Categorie Soggetti
Food Science & Tenology",Agriculture,"Chemistry Applied
ISSN journal
00218561
Volume
43
Issue
12
Year of publication
1995
Pages
3035 - 3041
Database
ISI
SICI code
0021-8561(1995)43:12<3035:TAOSPI>2.0.ZU;2-0
Abstract
Thermal behavior of soy protein isolates under different conditions of temperature, time, pH, protein concentration, and presence of reducin g agents was studied. Thermal treatments above 85 degrees C showed a d ecrease 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 treatment s tested led to modifications of the relative proportions either of th e high molecular weight aggregates (100-200 kDa) observed in the elect rophoretic profiles or of the alpha' and alpha subunits of beta-congly cinin. Increasing the pH to 9 or 10 and increasing the protein isolate concentration enhanced AB-11S aggregation during the thermal treatmen t. Either the presence of Na2SO3 or the pH 9-10 favored the beta-beta- conglycinin/B-glycinin aggregation. This interaction requires an incre ase of SH groups. Initially the beta-beta-conglycinin/B-glycinin aggre gates were stabilized by hydrophobic interactions and later by SS bond s.