Different source of commercial soy protein isolates: Structural, compositional, and physicochemical characteristics in relation to protein functionalities
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Different source of commercial soy protein isolates : Structural, compositional, and physicochemical characteristics in relation to protein functionalities. / Zhang, Longteng; Li, Qian; Zhang, Wei; Bakalis, Serafim; Luo, Yongkang; Lametsch, René.
In: Food Chemistry, Vol. 433, 137315, 2024.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Different source of commercial soy protein isolates
T2 - Structural, compositional, and physicochemical characteristics in relation to protein functionalities
AU - Zhang, Longteng
AU - Li, Qian
AU - Zhang, Wei
AU - Bakalis, Serafim
AU - Luo, Yongkang
AU - Lametsch, René
N1 - Publisher Copyright: © 2023 The Author(s)
PY - 2024
Y1 - 2024
N2 - This study aimed to illustrate the relationship among physicochemical properties, subunit composition and protein functionalities in a broad collection of commercial soy protein isolates (SPIs) from China and the EU. The results indicated that SPIs had large variations in glycinin/β-conglycinin composition, protein denaturation, and water- and oil-binding capacity (WBC and OBC) and solubility. These SPIs could be roughly divided into pre-denatured SPI, partially hydrolyzed SPI, and less modified SPI. The pre-denatured SPI with high surface hydrophobicity and large particle sizes showed reduced WBC and OBC due to increased protein aggregation, and partially hydrolyzed SPI showed high protein solubility owing to the exposure of hydrophilic regions and reduction in molecular size. The processing-induced physicochemical changes played a pivotal role in determining protein functionalities, whereas subunit composition affected protein functionality less. Overall, this study highlighted the obvious difference in raw material quality of commercial SPI, and provided promising methods for SPI categorization.
AB - This study aimed to illustrate the relationship among physicochemical properties, subunit composition and protein functionalities in a broad collection of commercial soy protein isolates (SPIs) from China and the EU. The results indicated that SPIs had large variations in glycinin/β-conglycinin composition, protein denaturation, and water- and oil-binding capacity (WBC and OBC) and solubility. These SPIs could be roughly divided into pre-denatured SPI, partially hydrolyzed SPI, and less modified SPI. The pre-denatured SPI with high surface hydrophobicity and large particle sizes showed reduced WBC and OBC due to increased protein aggregation, and partially hydrolyzed SPI showed high protein solubility owing to the exposure of hydrophilic regions and reduction in molecular size. The processing-induced physicochemical changes played a pivotal role in determining protein functionalities, whereas subunit composition affected protein functionality less. Overall, this study highlighted the obvious difference in raw material quality of commercial SPI, and provided promising methods for SPI categorization.
KW - Physicochemical properties
KW - Protein solubility
KW - Soy protein isolate
KW - Subunit composition
U2 - 10.1016/j.foodchem.2023.137315
DO - 10.1016/j.foodchem.2023.137315
M3 - Journal article
C2 - 37690138
AN - SCOPUS:85170437443
VL - 433
JO - Food Chemistry
JF - Food Chemistry
SN - 0308-8146
M1 - 137315
ER -
ID: 372526049