Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8891000 | LWT - Food Science and Technology | 2018 | 7 Pages |
Abstract
Effects of removal of non-network proteins by diffusion process on the storage modulus and loss modulus of soy protein isolate (SPI) gels and glycinin (11S) gels as a function of heating temperature and ionic strength were investigated. The composition of non-network proteins was determined by native-PAGE, non-reducing SDS-PAGE and reducing diagonal SDS-PAGE. Results showed that non-network proteins were composed of a majority of acid polypeptides (A), small amounts of AB subunits, soybean agglutinin, BowmanâBirk trypsin inhibitor, and lower amounts of αâ², α and A3 polypeptides. The results further revealed that 11S gels had higher ratios of non-network proteins than SPI gels, due to the increased ratio of A polypeptides in 11S gel. In addition, the removal of non-network proteins from the gel was found to have no effect on the storage modulus, but on the other hand resulted in a decrease in the loss modulus, suggesting that the loss modulus of the gel network is closely related to non-network proteins. This study presents an approach to investigate the changes of storage modulus and loss modulus of globular gels in relation to the removal of non-network proteins, and provides valuable information on the composition and content of these proteins in gel network formed at various conditions.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Food Science
Authors
Chao Wu, Willard Burton Navicha, Yufei Hua, Yeming Chen, Xiangzhen Kong, Caimeng Zhang,