We investigated the stability and rheological properties of extracts from soybean oil bodies (OB) obtained under different denaturing conditions (heating, guanidine hydrochloride, urea, and sodium dodecyl sulfate (SDS)). Differences in the interfacial and antioxidant properties exhibited by the different compositions of interfacial proteins in the extracted OB were also assessed. SDS disrupted the interfacial structure of OB, whereas the treatments under the other three denaturing conditions effectively increased the ability of the OB proteins to form a network structure. The analysis of the secondary and tertiary structures of proteins showed that all denaturation conditions affected both hydrogen bonding and hydrophobic interactions of the protein molecules, with urea leading to the most pronounced structural unfolding and rearrangement of the OB proteins. The microstructure results of the protein indicated that the protein treated with GuHCl and urea exhibited a 'shell-like' structure and structural decomposition, which can promote the pre-encapsulation of active substances through hydrogen bonding or hydrophobic interactions. The electrophoretic results further confirmed that SDS could displace 24-kDa proteins and disrupt the original membrane structure of OB, whereas urea removed most of the extrinsic proteins. The interfacial proteins extracted from OB using the four denaturing methods were different but all had enhanced interfacial and antioxidant properties compared to the control. Therefore, the extraction of OB under different denaturation conditions facilitated the hierarchical extraction of its interfacial proteins, thereby broadening its application in the food industry.
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