Physicochemical modifications of high-pressure-treated soybean protein isolates.
Changes induced by high pressure (HP) treatment (200-600 MPa) on soybean protein isolates (SPI) at pH 3 (SPI3) and pH 8 (SPI8) were analyzed. Changes in protein solubility, surface hydrophobicity (Ho), and free sulfhydryl content (SH(F)) were determined. Protein aggregation and denaturation and changes in secondary structure were also studied. An increase in protein Ho and aggregation, a reduction of free SH, and a partial unfolding of 7S and 11S fractions were observed in HP-treated SPI8. Changes in secondary structure were also detected, which led to a more disordered structure. HP-treated SPI3 was partially denatured and presented insoluble aggregates. A major molecular unfolding, a decrease of thermal stability, and an increase of protein solubility and Ho were also detected. At 400 and 600 MPa, a decrease of the SH(F) and a total denaturation were observed.
Puppo
Cecilia
C
Centro de Investigación y Desarrollo en Criotecnología de Alimentos (CIDCA) (UNLP - CONICET), 47 y 116, 1900 La Plata, Argentina.
Chapleau
Nicolas
N
Speroni
Francisco
F
De Lamballerie-Anton
Marie
M
Michel
F
F
Añón
Cristina
C
Anton
Marc
M
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004355:Drug Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D011312:Pressure; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D012995:Solubility; D030262:Soybean Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D013438:Sulfhydryl Compounds / Q000032:analysis
D030262:Soybean Proteins; D013438:Sulfhydryl Compounds